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 domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Heme oxygenase (preferred)
PDBe Complex ID:
PDB-CPX-159780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Heme oxygenase
Molecule details ›
Chains: A, B, C
Length: 215 amino acids
Theoretical weight: 24.17 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like
Length: 215 amino acids
Theoretical weight: 24.17 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P71119 (Residues: 1-215; Coverage: 100%)
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like
Ligands and Environments
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
SPRING-8 BEAMLINE BL41XU
Spacegroup:
P21
Expression system: Escherichia coli BL21(DE3)
