_EC 2.5.1.18 Glutathione transferase. 300 PDB entries  
EC 2.-.-.- Transferases. [17,772 PDB entries]
EC 2.5.-.- Transferring alkyl or aryl groups, other than methyl groups. [1,266 PDB entries]
EC 2.5.1.- Transferring alkyl or aryl groups, other than methyl groups. [1,266 PDB entries]
EC 2.5.1.18 Glutathione transferase. [300 PDB entries]    
10gs

Reaction: Rx + glutathione = hx + R-S-glutathione.
 


RX
+
glutathione
= HX
+
R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Glutathione S-alkyltransferase. Glutathione S-aralkyltransferase. Glutathione S-aryltransferase. S-(hydroxyalkyl)glutathione lyase.
Comments: A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; x may be a sulfate, nitrile or halide group. Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. Formerly Ec 1.8.6.1, Ec 2.5.1.12, Ec 2.5.1.13, Ec 2.5.1.14 and Ec 4.4.1.7.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 300 PDB entries in enzyme class E.C.2.5.1.18

  PDB code Protein
10gs
Human glutathione s-transferase p1-1, complex with ter117
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group VWW is 60.61% similar to enzyme reactant glutathione
11gs
Glutathione s-transferase complexed with ethacrynic acid-glu conjugate (form ii)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
12gs
Glutathione s-transferase complexed with s-nonyl-glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group 0HH is 68.97% similar to enzyme reactant glutathione
13gs
Glutathione s-transferase complexed with sulfasalazine
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
14gs
Glutathione s-transferase p1-1 apo form 1
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (194 residues) CATH domains: 3.40.30.10 1.20.1050.10
16gs
Glutathione s-transferase p1-1 apo form 3
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
17gs
Glutathione s-transferase p1-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
18gs
Glutathione s-transferase p1-1 complexed with 1-(s- glutathionyl)-2,4-dinitrobenzene
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN is 62.00% similar to enzyme reactant glutathione
19gs
Glutathione s-transferase p1-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1a0f
Crystal structure of glutathione s-transferase from escherichia coli complexed with glutathionesulfonic acid
Source: Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Gene: gst. Expressed in: escherichia coli k12. Expression_system_taxid: 83333.
Chains: A, B (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.00% similar to enzyme reactant glutathione
1ags
A surface mutant (g82r) of a human alpha-glutathione s- transferase shows decreased thermal stability and a new mode of molecular association in the crystal
Source: Synthetic construct. Organism_taxid: 32630. Organ: liver. Gene: pgth121-g82r. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (221 residues)
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1aqv
Glutathione s-transferase in complex with p-bromobenzylgluta
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytosol. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group 0HG is 71.43% similar to enzyme reactant glutathione
1aqw
Glutathione s-transferase in complex with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytosol. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1aqx
Glutathione s-transferase in complex with meisenheimer compl
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytosol. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTD is 57.14% similar to enzyme reactant glutathione
1aw9
Structure of glutathione s-transferase iii in apo form
Source: Zea mays. Organism_taxid: 4577. Variant: mutin. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
1axd
Structure of glutathione s-transferase-i bound with the liga lactoylglutathione
Source: Zea mays. Organism_taxid: 4577. Variant: mutin. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GGL is 45.00% similar to enzyme reactant glutathione
1b48
Crystal structure of mgsta4-4 in complex with gsh conjugate of 4-hydroxynonenal in one subunit and gsh in the other: evidence of signaling across dimer interface in mgsta4-4
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: lung. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: pet9a/mgsta4.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group HAG is 64.00% similar to enzyme reactant glutathione
1b4p
Crystal structures of class mu chimeric gst isoenzymes m1-2
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Strain: m5219. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: the enzyme is a chimeric gst, consisting of
Chain: A (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPS is 57.14% similar to enzyme reactant glutathione
1b8x
Glutathione s-transferase fused with the nuclear matrix targ signal of the transcription factor aml-1
Source: Escherichia coli. Organism_taxid: 562. Cell_line: bl21. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (260 residues) CATH domains: 3.40.30.10 1.20.1050.10 4.10.770.10
1bay
Glutathione s-transferase yfyf cys 47-carboxymethylated class pi, free enzyme
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: liver
Chains: A, B (193 residues) CATH domains: 3.40.30.10 1.20.1050.10
1bg5
Crystal structure of the ankyrin binding domain of alpha-na, k-atpase as a fusion protein with glutathione s-transferase
Source: Fragment: residues 219-254. Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: blood. Cellular_location: plasma membrane. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (254 residues) CATH domains: 3.40.30.10 1.20.1050.10 4.10.6.10
1bx9
Glutathione s-transferase in complex with herbicide
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Synthetic: yes
Chain: A (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GGL is 45.00% similar to enzyme reactant glutathione
1bye
Glutathione s-transferase i from mais in complex with atrazine glutathione conjugate
Source: Zea mays. Organism_taxid: 4577. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (213 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group ATA is 60.00% similar to enzyme reactant glutathione
1c72
Tyr115, gln165 and trp209 contribute to the 1,2-epoxy-3-(p- nitrophenoxy)propane conjugating activities of glutathione s-transferase cgstm1-1
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group EPY is 58.00% similar to enzyme reactant glutathione
1dug
Structure of the fibrinogen g chain integrin binding and factor xiiia crosslinking sites obtained through carrier protein driven crystallization
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: eukaryota. Metazoa. Platyhelminthes. Trematoda. Digenea. Strigeidida. Schistosomatoidea. Schistosomatidae. Schistosoma
Chains: A, B (234 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1e6b
Crystal structure of a zeta class glutathione s-transferase from arabidopsis thaliana
Source: Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (194 residues) CATH domains: 3.40.30.10 1.20.1050.10
1eem
Glutathione transferase from homo sapiens
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (237 residues) CATH domains: 3.40.30.10 1.20.1050.10
1eog
Crystal structure of pi class glutathione transferase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_organ: liver.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
1eoh
Glutathione transferase p1-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_organ: liver.
Chains: A, B, C, D, E, F, G, H (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
1ev4
Rat glutathione s-transferase a1-1: mutant w21f/f220y with g
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, C, D (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.96% similar to enzyme reactant glutathione
1ev9
Rat glutathione s-transferase a1-1 mutant w21f with gso3 bou
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, C, D (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.96% similar to enzyme reactant glutathione
1f2e
Structure of sphingomonad, glutathione s-transferase complex glutathione
Source: Sphingomonas paucimobilis. Organism_taxid: 13689. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
1f3a
Crystal structure of mgsta1-1 in complex with gsh
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1f3b
Crystal structure of mgsta1-1 in complex with glutathione conjugate of benzo[a]pyrene epoxide
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (222 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GBX is 46.00% similar to enzyme reactant glutathione
1fhe
Glutathione transferase (fh47) from fasciola hepatica
Source: Fasciola hepatica. Liver fluke. Organism_taxid: 6192. Organ: liver. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: secreted as a monomer, forms membrane-bound
Chain: A (214 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1fw1
Glutathione transferase zeta/maleylacetoacetate isomerase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1glp
1.8 angstroms molecular structure of mouse liver class pi glutathione s-transferase complexed with s-(p-nitrobenzyl) glutathione and other inhibitors
Source: Mus musculus. House mouse. Organism_taxid: 10090
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.00% similar to enzyme reactant glutathione
1glq
1.8 angstroms molecular structure of mouse liver class pi glutathione s-transferase complexed with s-(p-nitrobenzyl) glutathione and other inhibitors
Source: Mus musculus. House mouse. Organism_taxid: 10090
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTB is 66.00% similar to enzyme reactant glutathione
1gne
The three-dimensional structure of glutathione s-transferase schistosoma japonicum fused with a conserved neutralizing e gp41 of human immunodeficiency virus type 1
Source: Synthetic construct. Organism_taxid: 32630. Organ: liver. Gene: gp41.
Chain: A (232 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1gnw
Structure of glutathione s-transferase
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1gsb
New crystal forms of a mu class glutathione s-transferase from rat liver
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver
Chains: A, B, C, D (217 residues)
1gsc
New crystal forms of a mu class glutathione s-transferase from rat liver
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver
Chains: A, B, C, D (217 residues)
1gsd
Glutathione transferase a1-1 in unliganded form
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
1gse
Glutathione transferase a1-1 complexed with an ethacrynic ac glutathione conjugate (mutant r15k)
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1gsf
Glutathione transferase a1-1 complexed with ethacrynic acid
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
1gsq
Three-dimensional structure, catalytic properties and evolut sigma class glutathione transferase from squid, a progenito lens-crystallins of cephalopods
Source: Ommastrephes sloani pacificus. Organism_taxid: 6634. Strain: pacificus. Organ: digestive gland. Gene: cdna insert of clone pgst5. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (202 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN is 62.50% similar to enzyme reactant glutathione
1gss
Three-dimensional structure of class pi glutathione s-transf human placenta in complex with s-hexylglutathione at 2.8 an resolution
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: placenta
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group LEE is 76.92% similar to enzyme reactant glutathione
1gsu
An avian class-mu glutathione s-transferase, cgstm1-1 at 1.94 angstrom resolution
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Strain: leghorn. Tissue: liver. Gene: cgstm1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1gsy
Glutathione s-transferase yfyf, class pi, complexed with glu
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: liver. Other_details: glutathione commercially provided by sigma
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1gta
Crystal structures of a schistosomal drug and vaccine target glutathione s-transferase from schistosoma japonica and its with the leading antischistosomal drug praziquantel
Source: Schistosoma japonicum. Organism_taxid: 6182.
Chain: A (218 residues) CATH domains: 3.40.30.10 1.20.1050.10
1gtb
Crystal structures of a schistosomal drug and vaccine target: glutathione s-transferase from schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: pharmacia pgex-3x expression vector.
Chain: A (218 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group PZQ is 43.00% similar to enzyme reactant glutathione
1gti
Modified glutathione s-transferase (pi) complexed with s (p- nitrobenzyl)glutathione
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: liver. Cellular_location: cytoplasm
Chains: A, B, C, D, E, F (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTB is 66.00% similar to enzyme reactant glutathione
1gtu
Ligand-free human glutathione s-transferase m1a-1a
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: hela. Organ: liver. Cellular_location: cytoplasm. Gene: gstm1a. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
1guh
Structure determination and refinement of human alpha class glutathione transferase a1-1, and a comparison with the mu and pi class enzymes
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B, C, D (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSB is 74.00% similar to enzyme reactant glutathione
1guk
Crystal structure of murine alpha-class gsta4-4
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: lung. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (215 residues) CATH domains: 3.40.30.10 1.20.1050.10
1gul
Human glutathione transferase a4-4 complex with iodobenzyl g
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Tissue: substantia nigra. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
Chains: A, B, C, D, E, F, G, H (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GGL is 45.00% similar to enzyme reactant glutathione
1gum
Human glutathione transferase a4-4 without ligands
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: brain. Tissue: substantia nigra. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
1gwc
The structure of a tau class glutathione s-transferase from wheat, active in herbicide detoxification
Source: Aegilops tauschii. Bread wheat. Organism_taxid: 37682. Tissue: shoots. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21plyss. Other_details: wheat seedlings treated for 7 days with the wheat safener fenchlorazole-ethyl
Chains: A, B, C (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.92% similar to enzyme reactant glutathione
1hna
Crystal structure of human class mu glutathione transferase gstm2-2: effects of lattice packing on conformational heterogeneity
Source: Homo sapiens. Human. Organism_taxid: 9606
Chain: A (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN corresponds to enzyme reactant glutathione
1hnb
Crystal structure of human class mu glutathione transferase gstm2-2: effects of lattice packing on conformational heterogeneity
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN corresponds to enzyme reactant glutathione
1hnc
Crystal structure of human class mu glutathione transferase gstm2-2: effects of lattice packing on conformational heterogeneity
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN corresponds to enzyme reactant glutathione
1iyh
Crystal structure of hematopoietic prostaglandin d synthase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1iyi
Crystal structure of hematopoietic prostaglandin d synthase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1jlw
Anopheles dirus species b glutathione s-transferases 1-4
Source: Anopheles cracens. Organism_taxid: 123217. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
1k3l
Crystal structure analysis of s-hexyl-glutathione complex of glutathione transferase at 1.5 angstroms resolution
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1k3o
Crystal structure analysis of apo glutathione s-transferase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
1k3y
Crystal structure analysis of human glutathione s-transferas hexyl glutatione and glycerol at 1.3 angstrom
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.92% similar to enzyme reactant glutathione
1kbn
Glutathione transferase mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1lbk
Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional c-terminal helix of human class alpha isoenzyme
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1ljr
Glutathione transferase (hgst t2-2) from human
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (244 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1lqk
High resolution structure of fosfomycin resistance protein a (fosa)
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (134 residues) CATH domain: 3.10.180.10
1lqo
Crystal strutcure of the fosfomycin resistance protein a (fosa) containing bound thallium cations
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Gene: fosa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (134 residues) CATH domain: 3.10.180.10
1lqp
Crystal structure of the fosfomycin resistance protein (fosa) containing bound substrate
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Gene: fosa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (134 residues) CATH domain: 3.10.180.10
1lx2
Theoretical model of glutathione s-transferase p
Source: Macaca mulatta. Rhesus monkey
Chain: A (209 residues)
1m0u
Crystal structure of the drosophila glutathione s-transferas complex with glutathione
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (203 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1m99
Crystal structure of the 26 kda glutathione s-transferase fr schistosoma japonicum complexed with glutathione sulfonic a
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.96% similar to enzyme reactant glutathione
1m9a
Crystal structure of the 26 kda glutathione s-transferase fr schistosoma japonicum complexed with s-hexylglutathione
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.92% similar to enzyme reactant glutathione
1m9b
Crystal structure of the 26 kda glutathione s-transferase fr schistosoma japonicum complexed with gamma-glutamyl[s-(2-io cysteinyl]glycine
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group IBG is 71.43% similar to enzyme reactant glutathione
1md3
A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to alanine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1md4
A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1ml6
Crystal structure of mgsta2-2 in complex with the glutathione conjugate of benzo[a]pyrene-7(r),8(s)-diol- 9(s),10(r)-epoxide
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (220 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GBX is 46.00% similar to enzyme reactant glutathione
1mtc
Glutathione transferase mutant y115f
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPR is 57.00% similar to enzyme reactant glutathione
1n2a
Crystal structure of a bacterial glutathione transferase from escherichia coli with glutathione sulfonate in the active site
Source: Escherichia coli. Organism_taxid: 562. Gene: gt_1787923. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.00% similar to enzyme reactant glutathione
1nki
Crystal strucure of the fosfomycin resistance protein a (fos containing bound phosphonoformate
Source: Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (134 residues) CATH domain: 3.10.180.10
1nnr
Crystal structure of a probable fosfomycin resistance protei from pseudomonas aeruginosa with sulfate present in the act
Source: Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Gene: pa1129. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (134 residues) CATH domain: 3.10.180.10
1npb
Crystal structure of the fosfomycin resistance protein from tn2921
Source: Serratia marcescens. Organism_taxid: 615. Gene: tn2921. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D, E, F (140 residues) CATH domain: 3.10.180.10
1oe7
28kda glutathione s-transferase from schistosoma haematobium
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (204 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1oe8
28kda glutathione s-transferase from schistosoma haematobium (glutathione saturated)
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (204 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1okt
X-ray structure of glutathione s-transferase from the malarial parasite plasmodium falciparum
Source: Plasmodium falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: m15.
Chains: A, B (211 residues) CATH domains: 3.40.30.10 1.20.1050.10
1oyj
Crystal structure solution of rice gst1 (osgstu1) in complex glutathione.
Source: Oryza sativa. Rice. Organism_taxid: 4530. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (228 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1pa3
Crystal structure of glutathione-s-transferase from plasmodium falciparum
Source: Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (196 residues) CATH domains: 3.40.30.10 1.20.1050.10
1pd2
Crystal structure of hematopoietic prostaglandin d synthase with glutathione
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: spleen. Cellular_location: cytoplasm. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: de3.
Chains: 1, 2 (199 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1pgt
Crystal structure of human glutathione s-transferase p1- 1[v104] complexed with s-hexylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: 293. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1pkw
Crystal structure of human glutathione transferase (gst) a1- complex with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1pkz
Crystal structure of human glutathione transferase (gst) a1- 1
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domains: 3.40.30.10 1.20.1050.10
1pl1
Crystal structure of human glutathione transferase (gst) a1- 1 in complex with a decarboxy-glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group ABY is 58.00% similar to enzyme reactant glutathione
1pl2
Crystal structure of human glutathione transferase (gst) a1- 1 t68e mutant in complex with decarboxy-glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group ABY is 58.00% similar to enzyme reactant glutathione
1pmt
Glutathione transferase from proteus mirabilis
Source: Proteus mirabilis. Organism_taxid: 584. Cellular_location: periplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1pn9
Crystal structure of an insect delta-class glutathione s- transferase from a ddt-resistant strain of the malaria vector anopheles gambiae
Source: Anopheles gambiae. African malaria mosquito. Organism_taxid: 7165. Gene: gst1-6. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1px6
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1px7
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1q4j
Crystal structure of pf-gst1 with its inhibitor s-hexyl-gsh
Source: Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1r4w
Crystal structure of mitochondrial class kappa glutathione transferase
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: gsgstk1-1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (221 residues) CATH domain: 3.40.30.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1sfm
Structure of glutathione s- transferase of wuchereria bancrofti
Source: Wuchereria bancrofti. Agent of lymphatic filariasis
Chain: A (208 residues)
1sjo
Structure of glutathione s- transferase of brugia malayi
Source: Brugia malayi. Agent of lymphatic filariasis
Chain: A (208 residues)
1tdi
Crystal structure of hgsta3-3 in complex with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (218 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1tu7
Structure of onchocerca volvulus pi-class glutathione s-tran
Source: Onchocerca volvulus. Organism_taxid: 6282. Gene: gst2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1tu8
Structure of onchoverca volvulus pi-class glutathione s- transferase with its kompetitive inhibitor s-hexyl-gsh
Source: Onchocerca volvulus. Organism_taxid: 6282. Gene: gst2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1u3i
Crystal structure of glutathione s-tranferase from schistoso
Source: Schistosoma mansoni. Organism_taxid: 6183. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1u87
Crystal structure of the 26 kda glutathione s-transferase y7 from schistosoma japonicum complexed with glutathione
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1u88
Crystal structure of the 26 kda glutathione s-transferase y7f mutant from schistosoma japonicum complexed with s- octyl glutathione
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTY is 71.00% similar to enzyme reactant glutathione
1ua5
Non-fusion gst from s. Japonicum in complex with glutathione
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (215 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1usb
Rational design of a novel enzyme - efficient thioester hydrolysis enabled by the incorporation of a single his residue into human glutathione transferase a1-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (220 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1v2a
Glutathione s-transferase 1-6 from anopheles dirus species b
Source: Anopheles dirus. Organism_taxid: 7168. Gene: adgst1-6. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.96% similar to enzyme reactant glutathione
1v40
First inhibitor complex structure of human hematopoietic pro d synthase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1vf1
Cgsta1-1 in complex with glutathione
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: gta3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (226 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1vf2
Cgsta1-1 in complex with s-hexyl-glutathione
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: gta3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (225 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1vf3
Cgsta1-1 in complex with glutathione conjugate of cdnb
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: gta3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (225 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN is 62.00% similar to enzyme reactant glutathione
1vf4
Cgsta1-1 apo form
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: gta3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (227 residues) CATH domains: 3.40.30.10 1.20.1050.10
1xw5
Human glutathione s-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione, monoclinic crystal form
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm2, gst4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1xw6
1.9 angstrom resolution structure of human glutathione s- transferase m1a-1a complexed with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm1, gst1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1xwg
Human gst a1-1 t68e mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (213 residues) CATH domains: 3.40.30.10 1.20.1050.10
1xwk
2.3 angstrom resolution crystal structure of human glutathione s-transferase m1a-1a complexed with glutathionyl-s-dinitrobenzene
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm1, gst1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN is 62.00% similar to enzyme reactant glutathione
1y6e
Orthorhombic glutathione s-transferase of schistosoma japonicum
Source: Schistosoma japonicum. Organism_taxid: 6182. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Chains: A, B (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
1ydk
Crystal structure of the i219a mutant of human glutathione transferase a1-1 with s-hexylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (207 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
1yj6
Crystal structure of human glutathione s-transferase m1a-1a complexed with glutathionyl-zinc-trihydroxide
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm1, gst1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1ykc
Human glutathione s-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm2, gst4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDS is 50.00% similar to enzyme reactant glutathione
1yzx
Crystal structure of human kappa class glutathione transferase
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (218 residues) CATH domain: 3.40.30.10
Bound ligand:   Het Group GSF is 90.00% similar to enzyme reactant glutathione
1zgm
Crystal structure of putative glutathione s-transferase (15162326) from agrobacterium tumefaciens at 2.25 a resolution
Source: Agrobacterium tumefaciens str. C58. Bacteria. Expressed in: escherichia coli.
Chains: A, B (239 residues) CATH domain: 3.40.30.10
1zgn
Crystal structure of the glutathione transferase pi in complex with dinitrosyl-diglutathionyl iron complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
1zl9
Crystal structure of a major nematodE C.Elegans specific gst
Source: Caenorhabditis elegans. Organism_taxid: 6239. Gene: gst-5, ce01613. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (207 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
20gs
Glutathione s-transferase p1-1 complexed with cibacron blue
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: ubiquitous. Tissue: ubiquitous. Cell: ubiquitous. Cellular_location: cytosol. Gene: gstp1. Expressed in: escherichia coli.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
21gs
Human glutathione s-transferase p1-1 in complex with chlorambucil
Source: Homo sapiens. Human. Cellular_location: cytoplasm. Gene: gstp1. Expressed in: escherichia coli.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
22gs
Human glutathione s-transferase p1-1 y49f mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytoplasm. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
2a2r
Crystal structure of glutathione transferase pi in complex with s-nitrosoglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSN is 90.00% similar to enzyme reactant glutathione
2a2s
Crystal structure of human glutathione transferase in complex with s-nitrosoglutathione in the absence of reducing agent
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSN is 90.00% similar to enzyme reactant glutathione
2aaw
Studies on ligand binding and enzyme inhibition of plasmodium falciparum glutathione s-transferase
Source: Plasmodium falciparum. Malaria parasite p. Falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, C (205 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
2ab6
Human glutathione s-transferase m2-2 (E.C.2.5.1.18) complexed with s-methylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm2, gst4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSM is 95.00% similar to enzyme reactant glutathione
2c3n
Human glutathione-s-transferase t1-1, apo form
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (239 residues) CATH domains: 3.40.30.10 1.20.1050.10
2c3q
Human glutathione-s-transferase t1-1 w234r mutant, complex with s-hexylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (239 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
2c3t
Human glutathione-s-transferase t1-1, w234r mutant, apo form
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (239 residues) CATH domains: 3.40.30.10 1.20.1050.10
2c4j
Human glutathione-s-transferase m2-2 t210s mutant in complex with glutathione-styrene oxide conjugate
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSO is 68.00% similar to enzyme reactant glutathione
2c80
Structure of sh28gst in complex with s-hexyl glutathione
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.92% similar to enzyme reactant glutathione
2c8u
Structure of r21q mutant of sh28gst
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (202 residues) CATH domains: 3.40.30.10 1.20.1050.10
2ca8
Structure of sh28gst in complex with gsh at ph 6.0
Source: Schistosoma haematobium. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2cai
Structure of glutathione-s-transferase mutant, r21l, from schistosoma haematobium
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
2caq
Structure of r21l mutant of sh28gst in complex with gsh
Source: Schistosoma haematobium. Blood fluke. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (204 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2cvd
Crystal structure analysis of human hematopoietic prostaglan synthase complexed with hql-79
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2cz2
Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from mus musculus (form-1 cr
Source: Mus musculus. House mouse. Organism_taxid: 10090. Other_details: cell-free protein synthesis
Chain: A (212 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2cz3
Crystal structure of glutathione transferase zeta 1-1 (maleylacetoacetate isomerase) from mus musculus (form-2 cr
Source: Mus musculus. House mouse. Organism_taxid: 10090. Other_details: cell-free protein synthesis
Chains: A, B (191 residues) CATH domains: 3.40.30.10 1.20.1050.10
2dc5
Crystal structure of mouse glutathione s-transferase, mu7 (gstm7) at 1.6 a resolution
Source: Mus musculus. House mouse. Organism_taxid: 10090. Other_details: cell-free protein synthesis
Chains: A, B (218 residues) CATH domains: 3.40.30.10 1.20.1050.10
2dsa
Ternary complex of bphk, a bacterial gst
Source: Burkholderia xenovorans. Organism_taxid: 266265. Strain: lb400. Gene: bphk. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (200 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2f3m
Structure of human glutathione s-transferase m1a-1a complexed with 1-(s-(glutathionyl)-2,4,6- trinitrocyclohexadienate anion
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm1, gst1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D, E, F (218 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTD is 57.00% similar to enzyme reactant glutathione
2f8f
Crystal structure of the y10f mutant of the gluathione s-tra from schistosoma haematobium
Source: Schistosoma haematobium. Organism_taxid: 6185. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (203 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2fhe
Fasciola hepatica glutathione s-transferase isoform 1 in com glutathione
Source: Fasciola hepatica. Liver fluke. Organism_taxid: 6192. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2gdr
Crystal structure of a bacterial glutathione transferase
Source: Burkholderia xenovorans. Organism_taxid: 266265. Strain: lb400. Gene: bphk. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D, E, F (202 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2glr
Molecular structure at 1.8 angstroms of mouse liver class pi glutathione s-transferase complexed with s-(p- nitrobenzyl)glutathione and other inhibitors
Source: Mus musculus. House mouse. Organism_taxid: 10090
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
2gsq
Glutathione s-transferase from squid digestive gland complex (3-iodobenzyl)glutathione
Source: Ommastrephes sloani. Sloane's squid. Organism_taxid: 6633. Organ: digestive gland. Gene: cdna insert of clone pgst5. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (202 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GBI is 71.43% similar to enzyme reactant glutathione
2gsr
Structure of porcine class pi glutathione s-transferase
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: lung
Chains: A, B (207 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.96% similar to enzyme reactant glutathione
2gss
Human glutathione s-transferase p1-1 in complex with ethacrynic acid
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: ubiquitous. Cellular_location: cytoplasm. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
2gst
Structure of the xenobiotic substrate binding site of a glut transferase as revealed by x-ray crystallographic analysis complexes with the diastereomers of 9-(s-glutathionyl)-10-h 10-dihydrophenanthrene
Source: Rattus rattus. Black rat. Organism_taxid: 10117
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPS is 57.14% similar to enzyme reactant glutathione
2gtu
Ligand-free human glutathione s-transferase m2-2 (E.C.2.5.1.18), monoclinic crystal form
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: hela. Cellular_location: cytoplasm. Gene: gstm2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: the gstm2 cdna was amplified using rt-pcr
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
2h8a
Structure of microsomal glutathione transferase 1 in complex glutathione
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116
Chain: A (121 residues) CATH domain: 1.20.120.550
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2hnl
Structure of the prostaglandin d synthase from the parasitic onchocerca volvulus
Source: Onchocerca volvulus. Organism_taxid: 6282. Gene: gst1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (202 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2j9h
Crystal structure of human glutathione-s-transferase p1-1 cys-free mutant in complex with s-hexylglutathione at 2.4 a resolution
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
2ljr
Glutathione transferase apo-form from human
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (244 residues) CATH domains: 3.40.30.10 1.20.1050.10
2nto
Structure of the glutathione transferase from ochrobactrum a complex with glutathione
Source: Ochrobactrum anthropi. Organism_taxid: 529. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2oa7
Mouse c14a glutathione-s-transferase mutant in complex with s-hexyl glutathione
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: gstp1, gstpib. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
2oac
Mouse c14a glutathione-s-transferase mutant in complex with s-(p-nitrobenzyl) glutathione
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: gstp1, gstpib. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTB is 66.00% similar to enzyme reactant glutathione
2oad
Structure of glutathione-s-transferase c169a mutant
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: gstp1, gstpib. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTB is 66.00% similar to enzyme reactant glutathione
2pgt
Crystal structure of human glutathione s-transferase p1- 1[v104] complexed with (9r,10r)-9-(s-glutathionyl)-10- hydroxy-9,10-dihydrophenanthrene
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: 293. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPR is 57.00% similar to enzyme reactant glutathione
2pmt
Glutathione transferase from proteus mirabilis
Source: Proteus mirabilis. Organism_taxid: 584. Cellular_location: periplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2pvq
Crystal structure of ochrobactrum anthropi glutathione trans cys10ala mutant with glutathione bound at the h-site
Source: Ochrobactrum anthropi. Organism_taxid: 529. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2r3x
Crystal structure of an r15l hgsta1-1 mutant complexed with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.92% similar to enzyme reactant glutathione
2r6k
Crystal structure of an i71v hgsta1-1 mutant in complex with hexylglutathione
Source: Homo sapiens. Human. Gene: gsta1. Expressed in: escherichia coli.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
2vcq
Complex structure of prostaglandin d2 synthase at 1.95a.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vcr
Glutathione transferase a2-2 in complex with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
2vct
Glutathione transferase a2-2 in complex with delta-4- andostrene-3-17-dione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
2vcv
Glutathione transferase a3-3 in complex with glutathione and delta-4-androstene-3-17-dione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vcw
Complex structure of prostaglandin d2 synthase at 1.95a.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vcx
Complex structure of prostaglandin d2 synthase at 2.1a.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vcz
Complex structure of prostaglandin d2 synthase at 1.95a.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vd0
Complex structure of prostaglandin d2 synthase at 2.2a.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vd1
Complex structure of prostaglandin d2 synthase at 2.25a.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2vo4
Glutathione transferase from glycine max
Source: Glycine max. Soybean. Organism_taxid: 3847
Chains: A, B (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTB is 66.67% similar to enzyme reactant glutathione
2wb9
Fasciola hepatica sigma class gst
Source: Fasciola hepatica. Liver fluke. Organism_taxid: 6192. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2wdu
Fasciola hepatica sigma class gst
Source: Fasciola hepatica. Liver fluke. Organism_taxid: 6192. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDS is 50.00% similar to enzyme reactant glutathione
2wju
Glutathione transferase a2-2 in complex with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
2wrt
The 2.4 angstrom structure of the fasciola hepatica mu class gst, gst26
Source: Fasciola hepatica. Liver fluke. Organism_taxid: 6192. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D, E, F, G, H, I, J, K, L (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
3bby
Crystal structure of glutathione s-transferase (np_416804.1) escherichia coli k12 at 1.85 a resolution
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: yfcf, b2301, jw2298. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (191 residues) CATH domains: 3.40.30.10 1.20.1050.10
3crt
Structural characterization of an engineered allosteric protein
Source: Schistosoma japonicum. Blood fluke. Organism_taxid: 6182. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (214 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3cru
Structural characterization of an engineered allosteric protein
Source: Schistosoma japonicum. Blood fluke. Organism_taxid: 6182. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (214 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3csh
Crystal structure of glutathione transferase pi in complex w chlorambucil-glutathione conjugate
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1, faees3, gst3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group LZ6 is 52.63% similar to enzyme reactant glutathione
3csi
Crystal structure of the glutathione transferase pi allelic i104v/a113v, in complex with the chlorambucil-glutathione c
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1, faees3, gst3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group LZ6 is 52.63% similar to enzyme reactant glutathione
3csj
Human glutathione s-transferase p1-1 in complex with chlorambucil
Source: Homo sapiens. Human. Gene: gstp1, faees3, gst3. Expressed in: escherichia coli.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
3d0z
Structural charcaterization of an engineered allosteric protein
Source: Schistosoma japonicum. Blood fluke. Organism_taxid: 6182
Chain: A (214 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3dd3
Crystal structure of the glutathione transferase pi enzyme i with the bifunctional inhibitor, etharapta
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3dgq
Crystal structure of the glutathione transferase pi enzyme i with the bifunctional inhibitor, etharapta
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
3ee2
Structure of human prostaglandin d-synthase (hgsts1-1) in co nocodazole
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pgds. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3ein
Delta class gst
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: gstd1, gst, gst1, cg10045. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (207 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3erf
Crystal structure of gtt2 from saccharomyces cerevisiae
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: s288c. Gene: gtt2, l0560, yll060c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
3erg
Crystal structure of gtt2 from saccharomyces cerevisiae in c with glutathione sulfnate
Source: Saccharomyces cerevisiae. Organism_taxid: 4932. Strain: s288c. Gene: gtt2, l0560, yll060c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTS is 86.96% similar to enzyme reactant glutathione
3f6f
Crystal structure of glutathione transferase dmgstd10 from drosophila melanogaster
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: gstd10, dmel_cg18548. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
3fhs
Glutathione transferase from glycine max at 2.7 resolution
Source: Glycine max. Soybean. Organism_taxid: 3847. Gene: gst 4(gmgst4-4), gsta. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (216 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3fr3
Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Source: Plasmodium falciparum. Organism_taxid: 5833. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDS is 50.00% similar to enzyme reactant glutathione
3fr6
Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Source: Plasmodium falciparum. Organism_taxid: 5833. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
3fr9
Tetramerization and cooperativity in plasmodium falciparum g transferase are mediated by the atypic loop 113-118
Source: Plasmodium falciparum. Organism_taxid: 5833. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (200 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3frc
Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Source: Plasmodium falciparum. Organism_taxid: 5833. Gene: gst. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group 0HG is 71.00% similar to enzyme reactant glutathione
3fyg
Crystal structure of tetradeca-(3-fluorotyrosyl)- glutathione s-transferase
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Cell_line: bl21. Organ: liver. Gene: cdna insert of clone pgt33m. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPR is 57.00% similar to enzyme reactant glutathione
3gh6
Crystal structure of glutathione transferase dmgstd10 from d melanogaster, in complex with glutathione
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Cell_line: sl2 cell line. Gene: gstd10, dmel_cg18548. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3gss
Human glutathione s-transferase p1-1 in complex with ethacry glutathione conjugate
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: ubiquitous. Cellular_location: cytoplasm. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3gst
Structure of the xenobiotic substrate binding site of a glutathione s-transferase as revealed by x-ray crystallographic analysis of product complexes with the diastereomers of 9-(s-glutathionyl)-10-hydroxy-9, 10- dihydrophenanthrene
Source: Rattus rattus. Black rat. Organism_taxid: 10117
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPR is 57.00% similar to enzyme reactant glutathione
3gtu
Ligand-free heterodimeric human glutathione s-transferase m2-3 (ec 2.5.1.18), monoclinic crystal form
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: hela. Cellular_location: cytoplasm. Gene: gstm2, gstm3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: the gstm2 and gstm3 cdna were amplified
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
3gur
Crystal structure of mu class glutathione s-transferase (gst complex with glutathione and 6-(7-nitro-2,1,3-benzoxadiazol ylthio)hexanol (nbdhex)
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group BYG is 50.00% similar to enzyme reactant glutathione
3gus
Crystal strcture of human pi class glutathione s-transferase in complex with 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hex (nbdhex)
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3hjm
Crystal structure of human glutathione transferase pi y108v mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
3hjo
Crystal structure of glutathione transferase pi y108v mutant complex with the glutathione conjugate of ethacrynic acid
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3hkr
Crystal structure of glutathione transferase pi y108v mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
3i69
Apo glutathione transferase a1-1 gimf-helix mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D, E, F, G, H (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3i6a
Human gst a1-1 gimf mutant with glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D, E, F, G, H (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3ibh
Crystal structure of saccharomyces cerevisiae gtt2 in comple glutathione
Source: Saccharomyces cerevisiae. Organism_taxid: 4932. Strain: s288c. Gene: gtt2, l0560, yll060c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3ie3
Structural basis for the binding of the anti-cancer compound nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol (nbdhex) to huma glutathione s-transferases
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3ik7
Human glutathione transferase a4-4 with gsdhn
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta4. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group BOB is 64.00% similar to enzyme reactant glutathione
3ik9
Human gst a1-1-gimf with gsdhn
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D, E, F, G, H (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group BOB is 64.00% similar to enzyme reactant glutathione
3km6
Crystal structure of the human gst pi c47s/y108v double muta complex with the ethacrynic acid-glutathione conjugate
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: faees3, gst3, gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3kmn
Crystal structure of the human apo gst pi c47s/y108v double mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: faees3, gst3, gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
3kmo
Crystal structure of the human gst pi c47s/y108v double muta complex with the ethacrynic acid-glutathione conjugate (gro absence of the reducing agent dtt)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: faees3, gst3, gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3ktl
Crystal structure of an i71a human gsta1-1 mutant in complex hexylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
3kxo
An orally active inhibitor bound at the active site of hpgds
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptgds2, pgds. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3l0h
Crystal structure analysis of w21a mutant of human gsta1-1 i with s-hexylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (221 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
3lfl
Crystal structure of human glutathione transferase omega 1,
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto1, gsttlp28. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C (236 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3lg6
Crystal structure of putative glutathione transferase from coccidioides immitis
Source: Coccidioides immitis. Organism_taxid: 5501. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (229 residues) CATH domains: 3.40.30.10 1.20.1050.10
3ljr
Glutathione transferase (theta class) from human in complex with the glutathione conjugate of 1-menaphthyl sulfate
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (244 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GGC is 64.00% similar to enzyme reactant glutathione
3m1g
The structure of a putative glutathione s-transferase from corynebacterium glutamicum
Source: Corynebacterium glutamicum. Organism_taxid: 1718. Strain: atcc 13032. Gene: cg1426, cgl1264. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chains: A, B, C (297 residues) CATH domains: Unassigned 1.20.1050.10
3m3m
Crystal structure of glutathione s-transferase from pseudomo fluorescens [pf-5]
Source: Pseudomonas fluorescens. Organism_taxid: 220664. Strain: pf-5. Gene: pfl_4361. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (201 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3m8n
Crystal structure of a possible gutathione s-tranferase from rhodopseudomonas palustris
Source: Rhodopseudomonas palustris. Organism_taxid: 1076. Gene: gsta1, rpa4332. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (204 residues) CATH domains: 3.40.30.10 1.20.1050.10
3mak
Crystal structure of glutathione transferase dmgstd1 from dr melanogaster, in complex with glutathione
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: gstd1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3n5o
Crystal structure of putative glutathione transferase from coccidioides immitis bound to glutathione
Source: Coccidioides immitis. Organism_taxid: 5501. Gene: coi. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (228 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3n9j
Structure of human glutathione transferase pi class in compl ethacraplatin
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: faees3, gst3, gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
3o76
1.8 angstroms molecular structure of mouse liver glutathione transferase mutant c47a complexed with s-(p-nitrobenzyl)glu
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: gstp1, gstpib. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues)
Bound ligand:   Het Group GTB is 66.67% similar to enzyme reactant glutathione
3pgt
Crystal structure of hgstp1-1[i104] complexed with the gsh conjugate of (+)-anti-bpde
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: bl21 (de3) plyss. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GBX is 46.00% similar to enzyme reactant glutathione
3q18
Human glutathione transferase o2
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (236 residues) CATH domains: 3.40.30.10 1.20.1050.10
3q19
Human glutathione transferase o2
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (224 residues) CATH domains: 3.40.30.10 1.20.1050.10
3q74
Crystal structure analysis of the l7a mutant of the apo form alpha class glutathione transferase
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
3qag
Human glutathione transferase o2 with glutathione -new cryst
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (238 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3qmz
Crystal structure of the cytoplasmic dynein heavy chain moto
Source: Saccharomyces cerevisiae. Organism_taxid: 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932. Schistosoma japonicum. Organism_taxid: 6182. Expression_system_taxid: 4932
Chains: T, S (216 residues)
3rpn
Crystal structure of human kappa class glutathione transfera complex with s-hexylglutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstk1, hdcmd47p. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (220 residues) CATH domain: 3.40.30.10
Bound ligand:   Het Group GTX is 76.92% similar to enzyme reactant glutathione
3rpp
Crystal structure of human kappa class glutathione transfera form
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstk1, hdcmd47p. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (216 residues) CATH domain: 3.40.30.10
3tot
Crystal structure of glutathione transferase (target efi-501 ralstonia solanacearum gmi1000
Source: Ralstonia solanacearum. Organism_taxid: 305. Gene: gstk, rsc2721. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (212 residues) CATH domains: 3.40.30.10 1.20.1050.10
3tou
Crystal structure of glutathione transferase (target efi-501 ralstonia solanacearum gmi1000 with gsh bound
Source: Ralstonia solanacearum. Organism_taxid: 305. Gene: gstk, rsc2721. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (212 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3u6v
Crystal structure analysis of l23a mutant of human gst a1-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (207 residues) CATH domains: 3.40.30.10 1.20.1050.10
3uap
Crystal structure of glutathione transferase (target efi-501 methylococcus capsulatus str. Bath
Source: Methylococcus capsulatus. Organism_taxid: 243233. Strain: ncimb 11132 / bath. Atcc: 33009. Gene: gst, mca0074. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (203 residues) CATH domains: 3.40.30.10 1.20.1050.10
3uar
Crystal structure of glutathione transferase (target efi-501 methylococcus capsulatus str. Bath with gsh bound
Source: Methylococcus capsulatus. Organism_taxid: 243233. Strain: atcc 33009 / ncimb 11132 / bath. Gene: gst, mca0074. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (203 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3vi5
Human hematopoietic prostaglandin d synthase inhibitor compl structures
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hpgds, gsts, pgds, ptgds2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
3vi7
Human hematopoietic prostaglandin d synthase inhibitor compl structures
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hpgds, gsts, pgds, ptgds2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
3vln
Human glutathione transferase o1-1 c32s mutant in complex wi ascorbic acid
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto1, gsttlp28. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (239 residues) CATH domains: 3.40.30.10 1.20.1050.10
3vwx
Structural analysis of an epsilon-class glutathione s-transf housefly, musca domestica
Source: Musca domestica. House fly. Organism_taxid: 7370. Gene: gst-6b. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (218 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
3zfb
Crystal structure of the i75a mutant of human class alpha glutathione transferase in the apo form
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
3zfl
Crystal structure of the v58a mutant of human class alpha glutathione transferase in the apo form
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: plyss.
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
4acs
Crystal structure of mutant gst a2-2 with enhanced catalytic efficiency with azathioprine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 83333. Expression_system_variant: xl1-blue
Chains: A, B, C, D (219 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4ai6
Dynein motor domain - adp complex
Source: Schistosoma japonicum, saccharomyces cerevisiae. Organism_taxid: 6182, 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Chain: A (2650 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned 3.40.50.300 Unassigned 3.40.50.300 Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned 3.40.50.300
4akg
Dynein motor domain - atp complex
Source: Schistosoma japonicum, saccharomyces cerevisiae. Organism_taxid: 6182, 4932. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Chain: A (2650 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned 3.40.50.300 Unassigned 3.40.50.300 Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned 3.40.50.300
4akh
Dynein motor domain - amppnp complex
Source: Schistosoma japonicum, saccharomyces cerevisiae. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Chain: A (2650 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned 3.40.50.300 Unassigned 3.40.50.300 Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned 3.40.50.300
4aki
Dynein motor domain - luac derivative
Source: Schistosoma japonicum, saccharomyces cerevisiae. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Chain: A (2650 residues) CATH domains: Unassigned Unassigned Unassigned Unassigned 3.40.50.300 Unassigned 3.40.50.300 Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned Unassigned 3.40.50.300
4ec0
Crystal structure of hh-pgds with water displacing inhibitor
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsts, hpgds, pgds, ptgds2. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (199 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4ecb
Chimeric gst containing inserts of kininogen peptides
Source: Schistosoma japonicum, homo sapiens. Blood fluke, human. Organism_taxid: 6182, 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chains: A, B (202 residues) CATH domains: 3.40.30.10 1.20.1050.10
4ecc
Chimeric gst containing inserts of kininogen peptides
Source: Schistosoma japonicum, homo sapiens. Blood fluke, human. Organism_taxid: 6182, 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chain: A (206 residues) CATH domains: 3.40.30.10 1.20.1050.10
4edy
Crystal structure of hh-pgds with water displacing inhibitor
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsts, hpgds, pgds, ptgds2. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
4edz
Crystal structure of hh-pgds with water displacing inhibitor
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsts, hpgds, pgds, ptgds2. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C, D (198 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4ee0
Crystal structure of hh-pgds with water displacing inhibitor
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsts, hpgds, pgds, ptgds2. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (194 residues) CATH domains: 3.40.30.10 1.20.1050.10
4gss
Human glutathione s-transferase p1-1 y108f mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione
4gst
Reaction coordinate motion in an snar reaction catalyzed by glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTD is 57.00% similar to enzyme reactant glutathione
4gtu
Ligand-free homodimeric human glutathione s-transferase m4-4
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: hepg2. Cellular_location: cytoplasm. Gene: gstm4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: the gstm4 cdna was amplified using rt-pcr an
Chains: A, B, C, D, E, F, G, H (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
4hj2
Crystal structure analysis of gsta1-1 in complex with chlora
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsta1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
4ikh
Crystal structure of a glutathione transferase family member pseudomonas fluorescens pf-5, target efi-900003, with two g bound
Source: Pseudomonas protegens. Organism_taxid: 220664. Strain: pf-5. Gene: pfl_2287. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (227 residues) CATH domains: Unassigned 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4iq1
Crystal structure of glutathione s-transferase mha_0454 (tar 507015) from mannheimia haemolytica, substrate-free
Source: Mannheimia haemolytica phl213. Organism_taxid: 272629. Gene: mha_0454. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
4is0
Structural insights into omega-class glutathione transferase snapshot of enzyme reduction and identification of the non- ligandin site.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto1, gsttlp28. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (238 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDS is 50.00% similar to enzyme reactant glutathione
4iw9
Crystal structure of glutathione s-transferase mha_0454 (tar 507015) from mannheimia haemolytica, gsh complex
Source: Mannheimia haemolytica phl213. Organism_taxid: 272629. Gene: mha_0454. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4kf9
Crystal structure of a glutathione transferase family member ralstonia solanacearum, target efi-501780, with bound gsh c to a zinc ion, ordered active site
Source: Ralstonia solanacearum. Organism_taxid: 564066. Gene: gstg, rsipo_01298. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chain: A (318 residues) CATH domains: Unassigned 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4kgi
Crystal structure of a glutathione transferase family member shigella flexneri, target efi-507258, bound gsh, tev-his-ta in active site
Source: Shigella flexneri. Organism_taxid: 198215. Strain: 2a str. 2457t. Gene: gst, sf2457t_2570. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (200 residues) CATH domains: Unassigned 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4mdc
Crystal structure of glutathione s-transferase from sinorhiz meliloti 1021, nysgrc target 021389
Source: Sinorhizobium meliloti. Ensifer meliloti. Organism_taxid: 266834. Strain: 1021. Gene: gst4, r00327, smc00407. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (231 residues) CATH domains: Unassigned 1.20.1050.10
4mpf
Crystal structure of human glutathione transferase theta-2, with inorganic phosphate, gsh free, target efi-507257
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstt2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (243 residues) CATH domains: 3.40.30.10 1.20.1050.10
4mpg
Crystal structure of human glutathione transferase theta-2, with glutathione and unknown ligand, target efi-507257
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstt2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (243 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4nhw
Crystal structure of glutathione transferase smc00097 from sinorhizobium meliloti, target efi-507275, with one glutath per one protein subunit
Source: Sinorhizobium meliloti. Organism_taxid: 1286640. Gene: gst2, sm2011_c00097. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (213 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
4pgt
Crystal structure of hgstp1-1[v104] complexed with the gsh conjugate of (+)-anti-bpde
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: bl21 (de3) plyss. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (210 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GBX is 46.00% similar to enzyme reactant glutathione
4px1
Crystal structure of maleylacetoacetate isomerase from methy extorquens am1 with bound malonate (target efi-507068)
Source: Methylobacterium extorquens. Organism_taxid: 272630. Strain: atcc 14718 / dsm 1338 / am1. Gene: maia, mexam1_meta1p2830. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (217 residues) CATH domains: Unassigned 1.20.1050.10
4pxo
Crystal structure of maleylacetoacetate isomerase from methy extorquens am1 with bound malonate and gsh (target efi-5070
Source: Methylobacterium extorquens. Organism_taxid: 272630. Strain: atcc 14718 / dsm 1338 / am1. Gene: maia, mexam1_meta1p2830. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (216 residues) CATH domains: Unassigned 1.20.1050.10
5fwg
Tetra-(5-fluorotryptophanyl)-glutathione transferase
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Cell_line: bl21. Organ: liver. Gene: cdna insert of 3-3 (m1-1) enzy. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPR is 57.00% similar to enzyme reactant glutathione
5gss
Human glutathione s-transferase p1-1, complex with glutathio
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
5gst
Reaction coordinate motion in an snar reaction catalyzed by glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GDN is 62.00% similar to enzyme reactant glutathione
6gss
Human glutathione s-transferase p1-1, complex with glutathio
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
6gst
First-sphere and second-sphere electrostatic effects in the site of a class mu glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
6gsu
First-sphere and second-sphere electrostatic effects in the site of a class mu glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPS is 57.14% similar to enzyme reactant glutathione
6gsv
First-sphere and second-sphere electrostatic effects in the site of a class mu glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPS is 57.14% similar to enzyme reactant glutathione
6gsw
First-sphere and second-sphere electrostatic effects in the site of a class mu glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPS is 57.14% similar to enzyme reactant glutathione
6gsx
First-sphere and second-sphere electrostatic effects in the site of a class mu glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GPS is 57.14% similar to enzyme reactant glutathione
6gsy
First-sphere and second-sphere electrostatic effects in the site of a class mu glutathione transferase
Source: Rattus rattus. Black rat. Organism_taxid: 10117. Organ: liver. Gene: cdna insert of clone pgt33mx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (217 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
7gss
Human glutathione s-transferase p1-1, complex with glutathio
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
8gss
Human glutathione s-transferase p1-1, complex with glutathio
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B, C (209 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GSH corresponds to enzyme reactant glutathione
9gss
Human glutathione s-transferase p1-1, complex with s-hexyl glutathione
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Cellular_location: cytoplasm. Gene: gtp_human. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (208 residues) CATH domains: 3.40.30.10 1.20.1050.10
Bound ligand:   Het Group GTX is 76.00% similar to enzyme reactant glutathione