PDBsum entry 4gst

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Transferase PDB id
Protein chains
217 a.a. *
SO4 ×6
GTD ×2
Waters ×360
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Reaction coordinate motion in an snar reaction catalyzed by glutathione transferase
Structure: Glutathione s-transferase. Chain: a, b. Engineered: yes
Source: Rattus rattus. Black rat. Organism_taxid: 10117
Biol. unit: Dimer (from PQS)
1.90Å     R-factor:   0.180    
Authors: X.Ji,R.N.Armstrong,G.L.Gilliland
Key ref:
X.Ji et al. (1993). Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry, 32, 12949-12954. PubMed id: 8241147 DOI: 10.1021/bi00211a001
20-Jul-93     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P04905  (GSTM1_RAT) -  Glutathione S-transferase Mu 1
218 a.a.
217 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
Bound ligand (Het Group name = GTD)
matches with 57.00% similarity
= HX
+ R-S-glutathione
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   3 terms 
  Biological process     metabolic process   12 terms 
  Biochemical function     transferase activity     5 terms  


DOI no: 10.1021/bi00211a001 Biochemistry 32:12949-12954 (1993)
PubMed id: 8241147  
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.
X.Ji, R.N.Armstrong, G.L.Gilliland.
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21428697 A.Oakley (2011).
Glutathione transferases: a structural perspective.
  Drug Metab Rev, 43, 138-151.  
21079738 A.F.Kintzer, H.J.Sterling, I.I.Tang, E.R.Williams, and B.A.Krantz (2010).
Anthrax toxin receptor drives protective antigen oligomerization and stabilizes the heptameric and octameric oligomer by a similar mechanism.
  PLoS One, 5, e13888.  
  19662104 X.Ji, A.Pal, R.Kalathur, X.Hu, Y.Gu, J.E.Saavedra, G.S.Buzard, A.Srinivasan, L.K.Keefer, and S.V.Singh (2008).
Structure-Based Design of Anticancer Prodrug PABA/NO.
  Drug Des Devel Ther, 2, 123-130.  
16672236 J.L.Hearne, and R.F.Colman (2006).
Contribution of the mu loop to the structure and function of rat glutathione transferase M1-1.
  Protein Sci, 15, 1277-1289.  
16195544 J.L.Hearne, and R.F.Colman (2005).
Delineation of xenobiotic substrate sites in rat glutathione S-transferase M1-1.
  Protein Sci, 14, 2526-2536.  
12044179 J.Dong, P.R.Carey, Y.Wei, L.Luo, X.Lu, R.Q.Liu, and D.Dunaway-Mariano (2002).
Raman evidence for Meisenheimer complex formation in the hydrolysis reactions of 4-fluorobenzoyl- and 4-nitrobenzoyl-coenzyme A catalyzed by 4-chlorobenzoyl-coenzyme A dehalogenase.
  Biochemistry, 41, 7453-7463.  
11604524 A.J.Oakley, T.Harnnoi, R.Udomsinprasert, K.Jirajaroenrat, A.J.Ketterman, and M.C.Wilce (2001).
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B.
  Protein Sci, 10, 2176-2185.
PDB codes: 1jlv 1jlw
11123923 C.Micaloni, A.P.Mazzetti, M.Nuccetelli, J.Rossjohn, W.J.McKinstry, G.Antonini, A.M.Caccuri, A.J.Oakley, G.Federici, G.Ricci, M.W.Parker, and M.Lo Bello (2000).
Valine 10 may act as a driver for product release from the active site of human glutathione transferase P1-1.
  Biochemistry, 39, 15961-15970.  
10858281 S.A.McCallum, T.K.Hitchens, C.Torborg, and G.S.Rule (2000).
Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase.
  Biochemistry, 39, 7343-7356.  
10652317 Y.V.Patskovsky, L.N.Patskovska, and I.Listowsky (2000).
The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases.
  J Biol Chem, 275, 3296-3304.
PDB code: 2gtu
9929473 C.C.Chuang, S.H.Wu, S.H.Chiou, and G.G.Chang (1999).
Homology modeling of cephalopod lens S-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity.
  Biophys J, 76, 679-690.  
  10631991 L.O.Hansson, R.Bolton-Grob, M.Widersten, and B.Mannervik (1999).
Structural determinants in domain II of human glutathione transferase M2-2 govern the characteristic activities with aminochrome, 2-cyano-1,3-dimethyl-1-nitrosoguanidine, and 1,2-dichloro-4-nitrobenzene.
  Protein Sci, 8, 2742-2750.  
9817846 L.Prade, R.Huber, and B.Bieseler (1998).
Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase - explanations for the selectivity of the enzyme in plants.
  Structure, 6, 1445-1452.
PDB codes: 1bx9 1bye
9722558 L.Stella, A.M.Caccuri, N.Rosato, M.Nicotra, M.Lo Bello, F.De Matteis, A.P.Mazzetti, G.Federici, and G.Ricci (1998).
Flexibility of helix 2 in the human glutathione transferase P1-1. time-resolved fluorescence spectroscopy.
  J Biol Chem, 273, 23267-23273.  
9485454 M.Nicotra, M.Paci, M.Sette, A.J.Oakley, M.W.Parker, M.Lo Bello, A.M.Caccuri, G.Federici, and G.Ricci (1998).
Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure.
  Biochemistry, 37, 3020-3027.  
9368035 A.M.Caccuri, G.Antonini, M.Nicotra, A.Battistoni, M.Lo Bello, P.G.Board, M.W.Parker, and G.Ricci (1997).
Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina.
  J Biol Chem, 272, 29681-29686.  
  9007975 L.Hu, B.L.Borleske, and R.F.Colman (1997).
Probing the active site of alpha-class rat liver glutathione S-transferases using affinity labeling by monobromobimane.
  Protein Sci, 6, 43-52.  
9287168 L.O.Hansson, M.Widersten, and B.Mannervik (1997).
Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions.
  Biochemistry, 36, 11252-11260.  
9351803 L.Prade, R.Huber, T.H.Manoharan, W.E.Fahl, and W.Reuter (1997).
Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor.
  Structure, 5, 1287-1295.
PDB codes: 1aqv 1aqw 1aqx
9188738 R.T.Koehler, H.O.Villar, K.E.Bauer, and D.L.Higgins (1997).
Ligand-based protein alignment and isozyme specificity of glutathione S-transferase inhibitors.
  Proteins, 28, 202-216.  
9245401 X.Ji, M.Tordova, R.O'Donnell, J.F.Parsons, J.B.Hayden, G.L.Gilliland, and P.Zimniak (1997).
Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase.
  Biochemistry, 36, 9690-9702.
PDB codes: 1pgt 2pgt
8664265 G.Xiao, S.Liu, X.Ji, W.W.Johnson, J.Chen, J.F.Parsons, W.J.Stevens, G.L.Gilliland, and R.N.Armstrong (1996).
First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase.
  Biochemistry, 35, 4753-4765.
PDB codes: 6gst 6gsu 6gsv 6gsw 6gsx 6gsy
8710848 X.Ji, E.C.von Rosenvinge, W.W.Johnson, R.N.Armstrong, and G.L.Gilliland (1996).
Location of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallography.
  Proc Natl Acad Sci U S A, 93, 8208-8213.
PDB code: 2gsq
8591048 A.D.Cameron, I.Sinning, G.L'Hermite, B.Olin, P.G.Board, B.Mannervik, and T.A.Jones (1995).
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate.
  Structure, 3, 717-727.
PDB codes: 1gsd 1gse 1gsf
7667259 A.M.Gulick, and W.E.Fahl (1995).
Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme.
  Proc Natl Acad Sci U S A, 92, 8140-8144.  
7667397 A.M.Gulick, and W.E.Fahl (1995).
Mammalian glutathione S-transferase: regulation of an enzyme system to achieve chemotherapeutic efficacy.
  Pharmacol Ther, 66, 237-257.  
8789194 C.S.Poornima, and P.M.Dean (1995).
Hydration in drug design. 3. Conserved water molecules at the ligand-binding sites of homologous proteins.
  J Comput Aided Mol Des, 9, 521-531.  
7665611 L.Hu, and R.F.Colman (1995).
Monobromobimane as an affinity label of the xenobiotic binding site of rat glutathione S-transferase 3-3.
  J Biol Chem, 270, 21875-21883.  
  7774571 M.C.Wilce, P.G.Board, S.C.Feil, and M.W.Parker (1995).
Crystal structure of a theta-class glutathione transferase.
  EMBO J, 14, 2133-2143.  
7696312 P.Bico, J.Erhardt, W.Kaplan, and H.Dirr (1995).
Porcine class pi glutathione S-transferase: anionic ligand binding and conformational analysis.
  Biochim Biophys Acta, 1247, 225-230.  
  7538846 K.Lim, J.X.Ho, K.Keeling, G.L.Gilliland, X.Ji, F.Rüker, and D.C.Carter (1994).
Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV.
  Protein Sci, 3, 2233-2244.
PDB code: 1gne
7925413 P.Zimniak, B.Nanduri, S.Pikuła, J.Bandorowicz-Pikuła, S.S.Singhal, S.K.Srivastava, S.Awasthi, and Y.C.Awasthi (1994).
Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties.
  Eur J Biochem, 224, 893-899.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.