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PDBsum entry 1n0n

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
1n0n
Jmol
Contents
Protein chains
198 a.a. *
Ligands
SO4 ×4
Metals
_MN ×2
Waters ×337
* Residue conservation analysis
PDB id:
1n0n
Name: Oxidoreductase
Title: Catalytic and structural effects of amino-acid substitution in human manganese superoxide dismutase
Structure: Superoxide dismutase [mn]. Chain: a, b. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PDB file)
Resolution:
1.82Å     R-factor:   0.224     R-free:   0.241
Authors: G.E.O.Borgstahl,H.E.Parge,M.J.Hickey,W.F.Beyer Jr.,R.A.Halle J.A.Tainer
Key ref: G.E.O.Borgstahl et al. Catalytic and structural effects of amino-Acid substitution at his30 in human manganese superoxide dismutase. To be published, .
Date:
14-Oct-02     Release date:   06-Nov-02    
Supersedes: 1lus
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04179  (SODM_HUMAN) -  Superoxide dismutase [Mn], mitochondrial
Seq:
Struc:
222 a.a.
198 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.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!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     superoxide dismutase activity     2 terms