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PDBsum entry 3vln

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protein ligands links
Transferase PDB id
3vln
Jmol
Contents
Protein chain
239 a.a.
Ligands
SO4 ×3
ASC
GOL ×2
EDO
ACT
Waters ×205
PDB id:
3vln
Name: Transferase
Title: Human glutathione transferase o1-1 c32s mutant in complex wi ascorbic acid
Structure: Glutathione s-transferase omega-1. Chain: a. Synonym: gsto-1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gsto1, gsttlp28. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.182     R-free:   0.217
Authors: J.Brock,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:
02-Dec-11     Release date:   16-May-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P78417  (GSTO1_HUMAN) -  Glutathione S-transferase omega-1
Seq:
Struc:
241 a.a.
239 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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
Bound ligand (Het Group name = ASC)
corresponds exactly
= 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   13 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.