PDBe 1oyk

X-ray diffraction
2.59Å resolution

Crystal Structures of the Ferric, Ferrous, and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications

Released:

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09601 (Residues: 1-233; Coverage: 81%)
Gene names: HMOX1, HO, HO1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 55.665Å b: 77.662Å c: 100.318Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.309
Expression system: Escherichia coli