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PDBsum entry 3q18

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3q18
Jmol
Contents
Protein chain
236 a.a.
Ligands
PEG
GOL
Metals
_CL ×2
Waters ×345
PDB id:
3q18
Name: Transferase
Title: Human glutathione transferase o2
Structure: Glutathione s-transferase omega-2. Chain: a, b. Synonym: gsto-2. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.159     R-free:   0.186
Authors: H.Zhou,P.G.Board,A.J.Oakley
Key ref: H.Zhou et al. (2012). Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases. J Mol Biol, 420, 190-203. PubMed id: 22522127 DOI: 10.1016/j.jmb.2012.04.014
Date:
16-Dec-10     Release date:   25-Jan-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9H4Y5  (GSTO2_HUMAN) -  Glutathione S-transferase omega-2
Seq:
Struc:
243 a.a.
236 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: E.C.1.20.4.2  - Methylarsonate reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O
Methylarsonate
+ 2 × glutathione
= methylarsonite
+ glutathione disulfide
+ H(2)O
   Enzyme class 3: E.C.1.8.5.1  - Glutathione dehydrogenase (ascorbate).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate
2 × glutathione
+ 2 × dehydroascorbate
= glutathione disulfide
+ ascorbate
   Enzyme class 4: E.C.2.5.1.18  - Glutathione transferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RX + glutathione = HX + R-S-glutathione
2 × RX
+ 2 × glutathione
= HX
+ R-S-glutathione
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   3 terms 
  Biological process     metabolic process   9 terms 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2012.04.014 J Mol Biol 420:190-203 (2012)
PubMed id: 22522127  
 
 
Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases.
H.Zhou, J.Brock, D.Liu, P.G.Board, A.J.Oakley.
 
  ABSTRACT  
 
No abstract given.