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PDBsum entry 2wz5

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2wz5
Jmol
Contents
Protein chain
153 a.a. *
Ligands
SO4 ×3
MET ×2
Metals
_ZN ×3
_CU ×2
Waters ×394
* Residue conservation analysis
PDB id:
2wz5
Name: Oxidoreductase
Title: L38v sod1 mutant complexed with l-methionine.
Structure: Superoxide dismutase [cu-zn]. Chain: a, f. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
Resolution:
1.50Å     R-factor:   0.194     R-free:   0.255
Authors: S.V.Antonyuk,R.W.Strange,S.S.Hasnain
Key ref: S.Antonyuk et al. (2010). Structural discovery of small molecule binding sites in Cu-Zn human superoxide dismutase familial amyotrophic lateral sclerosis mutants provides insights for lead optimization. J Med Chem, 53, 1402-1406. PubMed id: 20067275 DOI: 10.1021/jm9017948
Date:
23-Nov-09     Release date:   08-Dec-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
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 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!
  Cellular component     extracellular region   16 terms 
  Biological process     reactive oxygen species metabolic process   62 terms 
  Biochemical function     antioxidant activity     12 terms  

 

 
    Added reference    
 
 
DOI no: 10.1021/jm9017948 J Med Chem 53:1402-1406 (2010)
PubMed id: 20067275  
 
 
Structural discovery of small molecule binding sites in Cu-Zn human superoxide dismutase familial amyotrophic lateral sclerosis mutants provides insights for lead optimization.
S.Antonyuk, R.W.Strange, S.S.Hasnain.
 
  ABSTRACT  
 
Dominant inheritance of point mutations in CuZn superoxide dismutase (SOD1) is the best characterized subset of familial amyotrophic lateral sclerosis (FALS) and accounts for some 20% of the known familial cases. We report the discovery and visualization via cocrystallography of two ligand-binding pockets in human SOD1 and its pathogenic mutants that have opened up the real possibility of undertaking lead compound discovery using a fragment-based approach for therapeutic purposes for SOD1 associated motor neuron disease.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20810277 M.Chruszcz, M.Domagalski, T.Osinski, A.Wlodawer, and W.Minor (2010).
Unmet challenges of structural genomics.
  Curr Opin Struct Biol, 20, 587-597.  
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