X-ray diffraction
2.1Å resolution

Comparisions of the Heme-Free and-Bound Crystal Structures of Human Heme Oxygenase-1


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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Heme oxygenase 1 soluble form Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 224 amino acids
Theoretical weight: 25.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P09601 (Residues: 1-224; Coverage: 78%)
Gene names: HMOX1, HO, HO1
Structure domains: Heme oxygenase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 76.211Å b: 55.507Å c: 108.001Å
α: 90° β: 98.88° γ: 90°
R R work R free
0.217 0.217 0.267
Expression system: Escherichia coli