PDBsum entry 4ff9

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chain
153 a.a.
_CU ×2
_ZN ×2
Waters ×24
PDB id:
Name: Oxidoreductase
Title: Crystal structure of cysteinylated wt sod1.
Structure: Superoxide dismutase [cu-zn]. Chain: a, b. Synonym: superoxide dismutase 1, hsod1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: sod1. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
2.50Å     R-factor:   0.282     R-free:   0.335
Authors: J.R.Auclair,H.R.Brodkin,J.A.D'Aquino,D.Ringe,G.A.Petsko,J.N.
Key ref: J.R.Auclair et al. (2013). Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase. Biochemistry, 52, 6145-6150. PubMed id: 23919400 DOI: 10.1021/bi400613h
31-May-12     Release date:   04-Sep-13    
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Protein chains
Pfam   ArchSchema ?
P00441  (SODC_HUMAN) -  Superoxide dismutase [Cu-Zn]
154 a.a.
153 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Superoxide dismutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 superoxide + 2 H+ = O2 + H2O2
2 × superoxide
+ 2 × H(+)
= O(2)
+ H(2)O(2)
      Cofactor: Iron or manganese or (zinc and copper)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   15 terms 
  Biological process     reactive oxygen species metabolic process   62 terms 
  Biochemical function     antioxidant activity     12 terms  


    Added reference    
DOI no: 10.1021/bi400613h Biochemistry 52:6145-6150 (2013)
PubMed id: 23919400  
Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase.
J.R.Auclair, H.R.Brodkin, J.A.D'Aquino, G.A.Petsko, D.Ringe, J.N.Agar.
The metalloenzyme Cu/Zn-superoxide dismutase (SOD1) catalyzes the reduction of superoxide anions into molecular oxygen and hydrogen peroxide. Hydrogen peroxide can oxidize SOD1, resulting in aberrant protein conformational changes, disruption of SOD1 function, and DNA damage. Cells may have evolved mechanisms of regulation that prevent such oxidation. We observed that cysteinylation of cysteine 111 (Cys111) of SOD1 prevents oxidation by peroxide (DOI 10.1021/bi4006122 ). In this article, we characterize cysteinylated SOD1 using differential scanning fluorometry and X-ray crystallography. The stoichiometry of binding was one cysteine per SOD1 dimer, and there does not appear to be free volume for a second cysteine without disrupting the dimer interface. Much of the three-dimensional structure of SOD1 is unaffected by cysteinylation. However, local conformational changes are observed in the cysteinylated monomer that include changes in conformation of the electrostatic loop (loop VII; residues 133-144) and the dimer interface (loop VI; residues 102-115). In addition, our data shows how cysteinylation precludes oxidation of cysteine 111 and suggests possible cross-talk between the dimer interface and the electrostatic loop.