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PDBsum entry 3ot7

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
3ot7
Jmol
Contents
Protein chains
205 a.a. *
Waters ×640
* Residue conservation analysis
PDB id:
3ot7
Name: Oxidoreductase
Title: Escherichia coli apo-manganese superoxide dismutase
Structure: Superoxide dismutase [mn]. Chain: a, b, c, d. Synonym: mnsod. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: soda, b3908, jw3879. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.194     R-free:   0.236
Authors: M.M.Whittaker,T.F.Lerch,O.Kirillova,M.S.Chapman,J.W.Whittake
Key ref: M.M.Whittaker et al. (2011). Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase. Arch Biochem Biophys, 505, 213-225. PubMed id: 21044611 DOI: 10.1016/j.abb.2010.10.021
Date:
10-Sep-10     Release date:   22-Dec-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00448  (SODM_ECOLI) -  Superoxide dismutase [Mn]
Seq:
Struc:
206 a.a.
205 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.15.1.1  - Superoxide dismutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 superoxide + 2 H+ = O2 + H2O2
2 × superoxide
+ 2 × H(+)
= O(2)
+ H(2)O(2)
      Cofactor: Fe cation or Mn(2+) or (Zn(2+) and Cu cation)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cellular response to selenium ion   7 terms 
  Biochemical function     antioxidant activity     6 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/j.abb.2010.10.021 Arch Biochem Biophys 505:213-225 (2011)
PubMed id: 21044611  
 
 
Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase.
M.M.Whittaker, T.F.Lerch, O.Kirillova, M.S.Chapman, J.W.Whittaker.
 
  ABSTRACT  
 
No abstract given.