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:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Heme oxygenase 1 (preferred)
PDBe Complex ID:
PDB-CPX-139216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1
Molecule details ›
Chains: A, B, C
Length: 267 amino acids
Theoretical weight: 30.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like
Length: 267 amino acids
Theoretical weight: 30.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
- Canonical:
P06762 (Residues: 1-267; Coverage: 92%)
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL41XU
Spacegroup:
P32
Expression system: Escherichia coli
