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PDBsum entry 3gzq

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3gzq
Jmol
Contents
Protein chains
123 a.a. *
125 a.a. *
Ligands
SO4 ×2
Waters ×251
* Residue conservation analysis
PDB id:
3gzq
Name: Oxidoreductase
Title: Human sod1 a4v metal-free variant
Structure: Superoxide dismutase [cu-zn]. Chain: a, b. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: sod1. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Resolution:
1.40Å     R-factor:   0.166     R-free:   0.193
Authors: A.Galaleldeen,A.B.Taylor,L.J.Whitson,P.J.Hart
Key ref: A.Galaleldeen et al. (2009). Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. Arch Biochem Biophys, 492, 40-47. PubMed id: 19800308
Date:
07-Apr-09     Release date:   13-Oct-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00441  (SODC_HUMAN) -  Superoxide dismutase [Cu-Zn]
Seq:
Struc:
154 a.a.
123 a.a.*
Protein chain
Pfam   ArchSchema ?
P00441  (SODC_HUMAN) -  Superoxide dismutase [Cu-Zn]
Seq:
Struc:
154 a.a.
124 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: 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   17 terms 
  Biological process     reactive oxygen species metabolic process   60 terms 
  Biochemical function     antioxidant activity     12 terms  

 

 
    Added reference    
 
 
Arch Biochem Biophys 492:40-47 (2009)
PubMed id: 19800308  
 
 
Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.
A.Galaleldeen, R.W.Strange, L.J.Whitson, S.V.Antonyuk, N.Narayana, A.B.Taylor, J.P.Schuermann, S.P.Holloway, S.S.Hasnain, P.J.Hart.
 
  ABSTRACT  
 
Amyotrophic lateral sclerosis (ALS) is a fatal, progressive neurodegenerative disease characterized by the destruction of motor neurons in the spinal cord and brain. A subset of ALS cases are linked to dominant mutations in copper-zinc superoxide dismutase (SOD1). The pathogenic SOD1 variants A4V and G93A have been the foci of multiple studies aimed at understanding the molecular basis for SOD1-linked ALS. The A4V variant is responsible for the majority of familial ALS cases in North America, causing rapidly progressing paralysis once symptoms begin and the G93A SOD1 variant is overexpressed in often studied murine models of the disease. Here we report the three-dimensional structures of metal-free A4V and of metal-bound and metal-free G93A SOD1. In the metal-free structures, the metal-binding loop elements are observed to be severely disordered, suggesting that these variants may share mechanisms of aggregation proposed previously for other pathogenic SOD1 proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21396374 E.A.Proctor, F.Ding, and N.V.Dokholyan (2011).
Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.
  J Mol Biol, 408, 555-567.  
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