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PDBsum entry 1px7

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1px7
Jmol
Contents
Protein chain
209 a.a. *
Ligands
MES ×2
GSH ×2
Metals
_CA
Waters ×418
* Residue conservation analysis
PDB id:
1px7
Name: Transferase
Title: A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate
Structure: Glutathione s-transferase p. Chain: a, b. Synonym: pi glutathione transferase, gst class-pi, gstp1-1. 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:
2.03Å     R-factor:   0.177     R-free:   0.218
Authors: G.K.-W.Kong,G.Polekhina,W.J.Mckinstry,M.W.Parker,B.Dragani, A.Aceto,D.Paludi,D.R.Principe,B.Mannervik,G.Stenberg
Key ref: G.K.-W.Kong et al. The multi-Functional role of a highly conserved aspartic acid residue in glutathione transferase p1-1. To be published, .
Date:
02-Jul-03     Release date:   22-Jul-03    
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 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
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   9 terms 
  Biological process     metabolic process   31 terms 
  Biochemical function     S-nitrosoglutathione binding     8 terms