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PDBsum entry 2vcr

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2vcr
Jmol
Contents
Protein chains
(+ 2 more) 221 a.a. *
Ligands
GSW ×8
Waters ×549
* Residue conservation analysis
Superseded by: 2wju
PDB id:
2vcr
Name: Transferase
Title: Glutathione transferase a2-2 in complex with glutathione
Structure: Glutathione s-transferase a2. Chain: a, b, c, d, e, f, g, h. Synonym: glutathione-s-transferase a2-2, gth2, ha subunit 2, gst-gamma, gsta2-2, gst class-alpha member 2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.226     R-free:   0.275
Authors: K.Tars,B.Olin,B.Mannervik
Key ref: K.Tars et al. Structural basis of steroid isomerase activity of alpha class glutathione transferases. To be published, .
Date:
26-Sep-07     Release date:   28-Oct-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09210  (GSTA2_HUMAN) -  Glutathione S-transferase A2
Seq:
Struc:
222 a.a.
221 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

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