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PDBsum entry 2ab6

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2ab6
Jmol
Contents
Protein chain
217 a.a. *
Ligands
GSM ×4
Waters ×203
* Residue conservation analysis
PDB id:
2ab6
Name: Transferase
Title: Human glutathione s-transferase m2-2 (E.C.2.5.1.18) complexed with s-methylglutathione
Structure: Glutathione s-transferase mu 2. Chain: a, b, c, d. Synonym: gstm2-2, gst class-mu 2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gstm2, gst4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
Resolution:
2.50Å     R-factor:   0.230     R-free:   0.280
Authors: Y.Patskovsky,S.C.Almo,I.Listowsky
Key ref: Y.Patskovsky et al. Structural perturbations in the active site of human glutathione-S-Transferase m2-2 upon ligand binding. To be published, .
Date:
14-Jul-05     Release date:   02-Aug-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P28161  (GSTM2_HUMAN) -  Glutathione S-transferase Mu 2
Seq:
Struc:
218 a.a.
217 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
RX
+
glutathione
Bound ligand (Het Group name = GSM)
matches with 95.00% 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     cytoplasm   4 terms 
  Biological process     metabolic process   15 terms 
  Biochemical function     transferase activity     6 terms