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PDBsum entry 2lu5

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protein metals links
Oxidoreductase PDB id
2lu5
Jmol
Contents
Protein chain
153 a.a.
Metals
_CU
PDB id:
2lu5
Name: Oxidoreductase
Title: Structure and chemical shifts of cu(i),zn(ii) superoxide dis solid-state nmr
Structure: Superoxide dismutase [cu-zn]. Chain: a. Synonym: superoxide dismutase 1, hsod1. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: sod1. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 19 models
Authors: M.J.Knight,A.J.Pell,I.Bertini,I.C.Felli,L.Gonnelli,R.Pieratt T.Herrmann,L.Emsley,G.Pintacuda
Key ref: M.J.Knight et al. (2012). Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR. Proc Natl Acad Sci U S A, 109, 11095-11100. PubMed id: 22723345 DOI: 10.1073/pnas.1204515109
Date:
08-Jun-12     Release date:   27-Jun-12    
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 2 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   16 terms 
  Biological process     reactive oxygen species metabolic process   62 terms 
  Biochemical function     antioxidant activity     12 terms  

 

 
    Added reference    
 
 
DOI no: 10.1073/pnas.1204515109 Proc Natl Acad Sci U S A 109:11095-11100 (2012)
PubMed id: 22723345  
 
 
Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR.
M.J.Knight, A.J.Pell, I.Bertini, I.C.Felli, L.Gonnelli, R.Pierattelli, T.Herrmann, L.Emsley, G.Pintacuda.
 
  ABSTRACT  
 
No abstract given.