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PDBsum entry 4aun

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4aun
Jmol
Contents
Protein chains
(+ 2 more) 671 a.a.
Ligands
HDD ×8
Metals
_CA ×9
Waters ×3405
PDB id:
4aun
Name: Oxidoreductase
Title: Crystal structure, recombinant expression and mutagenesis studies of the bifunctional catalase-phenol oxidase from scytalidium thermophilum
Structure: Catalase-phenol oxidase. Chain: a, b, c, d, e, f, g, h. Engineered: yes
Source: Scytalidium thermophilum. Organism_taxid: 85995. Atcc: 16454. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star.
Resolution:
1.92Å     R-factor:   0.166     R-free:   0.200
Authors: Y.Yuzugullu,C.H.Trinh,M.A.Smith,A.R.Pearson,S.E.V.Phillips, D.Sutay Kocabas,U.Bakir,Z.B.Ogel,M.J.Mcpherson
Key ref: Y.Yuzugullu et al. (2013). Structure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from Scytalidium thermophilum. Acta Crystallogr D Biol Crystallogr, 69, 398-408. PubMed id: 23519415 DOI: 10.1107/S0907444912049001
Date:
18-May-12     Release date:   27-Feb-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
M4GGR8  (M4GGR8_9PEZI) -  Catalase
Seq:
Struc:
 
Seq:
Struc:
699 a.a.
671 a.a.
Key:    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 = HDD) matches with 93.33% similarity
Mn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444912049001 Acta Crystallogr D Biol Crystallogr 69:398-408 (2013)
PubMed id: 23519415  
 
 
Structure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from Scytalidium thermophilum.
Y.Yuzugullu, C.H.Trinh, M.A.Smith, A.R.Pearson, S.E.Phillips, D.Sutay Kocabas, U.Bakir, Z.B.Ogel, M.J.McPherson.
 
  ABSTRACT  
 
No abstract given.