spacer
spacer

PDBsum entry 4b2y

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4b2y
Jmol
Contents
Protein chains
675 a.a.
Ligands
HEM ×4
Metals
_CA ×6
Waters ×1804
PDB id:
4b2y
Name: Oxidoreductase
Title: Probing the active center of catalase-phenol oxidase from scytalidium thermophilum
Structure: Catalase-phenol oxidase. Chain: a, b, c, d. Engineered: yes. Other_details: covalent bond cys123 to his83 ce1
Source: Scytalidium thermophilum. Organism_taxid: 85995. Atcc: 16454. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star.
Resolution:
1.90Å     R-factor:   0.151     R-free:   0.181
Authors: Y.Yuzugullu,C.H.Trinh,A.R.Pearson,Z.B.Ogel,M.J.Mcpherson
Key ref: Y.Yuzugullu et al. (2013). Investigating the active centre of the Scytalidium thermophilum catalase. Acta Crystallogr Sect F Struct Biol Cryst Commun, 69, 369-375. PubMed id: 23545640 DOI: 10.1107/S1744309113004211
Date:
19-Jul-12     Release date:   10-Apr-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
R4GRT6  (R4GRT6_9PEZI) -  Catalase
Seq:
Struc:
 
Seq:
Struc:
699 a.a.
675 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; Manganese
Heme
Bound ligand (Het Group name = HEM) matches with 95.45% similarity
Manganese
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/S1744309113004211 Acta Crystallogr Sect F Struct Biol Cryst Commun 69:369-375 (2013)
PubMed id: 23545640  
 
 
Investigating the active centre of the Scytalidium thermophilum catalase.
Y.Yuzugullu, C.H.Trinh, L.Fairhurst, Z.B.Ogel, M.J.McPherson, A.R.Pearson.
 
  ABSTRACT  
 
No abstract given.