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PDBsum entry 1kbn

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protein ligands Protein-protein interface(s) links
Transferase PDB id
1kbn
Jmol
Contents
Protein chain
209 a.a. *
Ligands
GSH ×2
MES ×2
GOL ×2
Waters ×321
* Residue conservation analysis
PDB id:
1kbn
Name: Transferase
Title: Glutathione transferase mutant
Structure: Glutathione s-transferase p. Chain: a, b. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.226     R-free:   0.244
Authors: J.Rossjohn,M.W.Parker
Key ref: J.Rossjohn and m.w.parker Crystal structure of glutathione transferase mutant. To be published, .
Date:
06-Nov-01     Release date:   11-Nov-03    
PROCHECK
Go to PROCHECK summary
 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
Bound ligand (Het Group name = GSH)
corresponds exactly
= 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   6 terms 
  Biological process     metabolic process   32 terms 
  Biochemical function     S-nitrosoglutathione binding     8 terms