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PDBsum entry 4bcz

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
4bcz
Jmol
Contents
Protein chain
110 a.a.
Waters ×147
PDB id:
4bcz
Name: Oxidoreductase
Title: Monomeric human cu,zn superoxide dismutase, loops iv and vii deleted, apo form.
Structure: Superoxide dismutase [cu-zn]. Chain: a, b. Fragment: residues 2049,83-124,141-154. Synonym: superoxide dismutase 1, hsod1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.93Å     R-factor:   0.171     R-free:   0.219
Authors: K.Saraboji,W.Awad,J.Danielsson,L.Lang,M.Kurnik,S.L.Marklund, M.Oliveberg,D.T.Logan
Key ref: J.Danielsson et al. (2013). Global structural motions from the strain of a single hydrogen bond. Proc Natl Acad Sci U S A, 110, 3829-3834. PubMed id: 23431167 DOI: 10.1073/pnas.1217306110
Date:
03-Oct-12     Release date:   27-Feb-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00441  (SODC_HUMAN) -  Superoxide dismutase [Cu-Zn]
Seq:
Struc:
154 a.a.
110 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 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!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     metal ion binding     1 term  

 

 
    Added reference    
 
 
DOI no: 10.1073/pnas.1217306110 Proc Natl Acad Sci U S A 110:3829-3834 (2013)
PubMed id: 23431167  
 
 
Global structural motions from the strain of a single hydrogen bond.
J.Danielsson, W.Awad, K.Saraboji, M.Kurnik, L.Lang, L.Leinartaite, S.L.Marklund, D.T.Logan, M.Oliveberg.
 
  ABSTRACT  
 
No abstract given.