4wd4

X-ray diffraction
2.95Å resolution

Crystal structure of human HO1 H25R

Released:
Source organism: Homo sapiens

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-140706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 292 amino acids
Theoretical weight: 33.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09601 (Residues: 1-288; Coverage: 100%)
Gene names: HMOX1, HO, HO1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 74.08Å b: 54.41Å c: 122.28Å
α: 90° β: 99.09° γ: 90°
R-values:
R R work R free
0.206 0.203 0.259
Expression system: Escherichia coli