PDBe 5btq

X-ray diffraction
2.08Å resolution

Crystal structure of human heme oxygenase 1 H25R with biliverdin bound

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

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 27.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 61.7Å b: 54.74Å c: 72.51Å
α: 90° β: 99.37° γ: 90°
R-values:
R R work R free
0.185 0.183 0.228
Expression system: Escherichia coli BL21