› 4gpc

X-ray diffraction
1.85Å resolution

Structure of the biliverdin-HmuO, heme oxygenase from Corynebacterium diphtheriae

Released:
DOI: 10.2210/pdb4gpc/pdb
PDB entry 4gpc coloured by chain, front view.
PDB entry 4gpc coloured by chain, side view.
PDB entry 4gpc coloured by chain, top view.
Source organism: Corynebacterium diphtheriae
Entry authors: Unno M, Ikeda-Saito M

Function and Biology Details

Reaction catalysed: 
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-560537 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
heme oxygenase (biliverdin-producing) Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 215 amino acids
Theoretical weight: 24.17 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54AI1 (Residues: 1-215; Coverage: 100%)
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand ASC 1 x ASC
2 bound ligands:
Ligand BLA 3 x BLA
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P21
Unit cell:
a: 54.114Å b: 63.091Å c: 107.558Å
α: 90° β: 100.73° γ: 90°
R-values:
R R work R free
0.17 0.168 0.203
Expression system: Escherichia coli

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