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PDBsum entry 3kmn

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3kmn
Jmol
Contents
Protein chain
209 a.a. *
Ligands
CO3 ×2
PO4
Metals
_CA ×6
Waters ×482
* Residue conservation analysis
PDB id:
3kmn
Name: Transferase
Title: Crystal structure of the human apo gst pi c47s/y108v double mutant
Structure: Glutathione s-transferase p. Chain: a, b. Synonym: gst class-pi, gstp1-1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: faees3, gst3, gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.173     R-free:   0.210
Authors: L.J.Parker
Date:
11-Nov-09     Release date:   23-Mar-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P09211  (GSTP1_HUMAN) -  Glutathione S-transferase P
Seq:
Struc:
210 a.a.
209 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     TRAF2-GSTP1 complex   9 terms 
  Biological process     metabolic process   31 terms 
  Biochemical function     S-nitrosoglutathione binding     8 terms