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PDBsum entry 3re8

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3re8
Jmol
Contents
Protein chains
499 a.a.
Ligands
HEM ×4
Waters ×1283
PDB id:
3re8
Name: Oxidoreductase
Title: Structural and kinetic analysis of the beef liver catalase i with nitric oxide
Structure: Catalase. Chain: a, b, c, d. Fragment: unp residues 4-502. Ec: 1.11.1.6
Source: Bos taurus. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913. Other_details: liver
Resolution:
1.90Å     R-factor:   0.221     R-free:   0.259
Authors: N.Purwar,M.Schmidt
Key ref: N.Purwar et al. (2011). Interaction of nitric oxide with catalase: structural and kinetic analysis. Biochemistry, 50, 4491-4503. PubMed id: 21524057 DOI: 10.1021/bi200130r
Date:
03-Apr-11     Release date:   25-May-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00432  (CATA_BOVIN) -  Catalase
Seq:
Struc:
 
Seq:
Struc:
527 a.a.
499 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.11.1.6  - Catalase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 H2O2 = O2 + 2 H2O
2 × H(2)O(2)
= O(2)
+ 2 × H(2)O
      Cofactor: Heme; Mn(2+)
Heme
Bound ligand (Het Group name = HEM) matches with 95.45% similarity
Mn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   6 terms 
  Biological process     oxidation-reduction process   17 terms 
  Biochemical function     antioxidant activity     12 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi200130r Biochemistry 50:4491-4503 (2011)
PubMed id: 21524057  
 
 
Interaction of nitric oxide with catalase: structural and kinetic analysis.
N.Purwar, J.M.McGarry, J.Kostera, A.A.Pacheco, M.Schmidt.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22338689 M.Schmidt, V.Šrajer, N.Purwar, and S.Tripathi (2012).
The kinetic dose limit in room-temperature time-resolved macromolecular crystallography.
  J Synchrotron Radiat, 19, 264-273.  
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