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PDBsum entry 3qgp

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3qgp
Jmol
Contents
Protein chains
110 a.a.
Ligands
HEM-CYN ×2
Metals
_MG ×2
Waters ×252
PDB id:
3qgp
Name: Oxidoreductase
Title: Crystal structure of isdi in complex with heme and cyanide
Structure: Heme-degrading monooxygenase isdi. Chain: a, b. Synonym: heme oxygenase, iron-regulated surface determinant iron-responsive surface determinant isdi. Engineered: yes
Source: Staphylococcus aureus subsp. Aureus n3 organism_taxid: 158879. Strain: n315. Gene: isdi, sa0160. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.80Å     R-factor:   0.176     R-free:   0.196
Authors: G.N.Ukpabi,M.E.P.Murphy
Key ref: S.J.Takayama et al. Heme ruffling enables the catalytic activity of the h degrading enzyme isdi. To be published, .
Date:
24-Jan-11     Release date:   20-Jul-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7A827  (ISDI_STAAN) -  Heme oxygenase (staphylobilin-producing) 2
Seq:
Struc:
108 a.a.
110 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.14.99.48  - Heme oxygenase (staphylobilin-producing).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. Protoheme + 4 AH2 + 4 O2 = 5-oxo-delta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
2. Protoheme + 4 AH2 + 4 O2 = 15-oxo-beta-bilirubin + Fe2+ + CO + 4 A + 4 H2O
Protoheme
Bound ligand (Het Group name = HEM)
matches with 95.45% similarity
+ 4 × AH(2)
+ 4 × O(2)
= 5-oxo-delta-bilirubin
+ Fe(2+)
+ CO
+ 4 × A
+ 4 × H(2)O
Protoheme
+ 4 × AH(2)
+ 4 × O(2)
= 15-oxo-beta-bilirubin
+ Fe(2+)
+ CO
+ 4 × A
+ 4 × H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   3 terms 
  Biochemical function     oxidoreductase activity     7 terms