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PDBsum entry 2xjk

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protein metals links
Oxidoreductase PDB id
2xjk
Jmol
Contents
Protein chain
153 a.a. *
Metals
_ZN ×4
_CU
Waters ×153
* Residue conservation analysis
PDB id:
2xjk
Name: Oxidoreductase
Title: Monomeric human cu,zn superoxide dismutase
Structure: Superoxide dismutase [cu-zn]. Chain: a. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.45Å     R-factor:   0.167     R-free:   0.199
Authors: K.Saraboji,L.Leinartaite,A.Nordlund,M.Oliveberg,D.T.Logan
Key ref: L.Leinartaite et al. (2010). Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1. J Am Chem Soc, 132, 13495-13504. PubMed id: 20822138 DOI: 10.1021/ja1057136
Date:
07-Jul-10     Release date:   01-Sep-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00441  (SODC_HUMAN) -  Superoxide dismutase [Cu-Zn]
Seq:
Struc:
154 a.a.
153 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 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     extracellular region   20 terms 
  Biological process     cellular response to potassium ion   66 terms 
  Biochemical function     antioxidant activity     13 terms  

 

 
    Added reference    
 
 
DOI no: 10.1021/ja1057136 J Am Chem Soc 132:13495-13504 (2010)
PubMed id: 20822138  
 
 
Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1.
L.Leinartaite, K.Saraboji, A.Nordlund, D.T.Logan, M.Oliveberg.
 
  ABSTRACT  
 
No abstract given.