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PDBsum entry 2aqn

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2aqn
Jmol
Contents
Protein chains
155 a.a. *
Ligands
SO4
Metals
_CU ×2
CU1 ×3
_ZN ×3
Waters ×530
* Residue conservation analysis
PDB id:
2aqn
Name: Oxidoreductase
Title: Cu/zn superoxide dismutase from neisseria meningitidis
Structure: Superoxide dismutase [cu-zn]. Chain: a, b, c. Engineered: yes
Source: Neisseria meningitidis. Organism_taxid: 487. Gene: sodc. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PDB file)
Resolution:
1.40Å     R-factor:   0.128     R-free:   0.190
Authors: M.Didonato,C.J.Kassmann,C.K.Bruns,D.E.Cabelli,Z.Cao, L.B.Tabatabai,J.S.Kroll,E.D.Getzoff
Key ref: M.Didonato et al. Cu/zn superoxide dismutase from neisseria meningitidis. To be published, .
Date:
18-Aug-05     Release date:   31-Oct-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P57005  (SODC_NEIMA) -  Superoxide dismutase [Cu-Zn]
Seq:
Struc:
186 a.a.
155 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     periplasmic space   1 term 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     antioxidant activity     4 terms