3moo

X-ray diffraction
1.71Å resolution

Crystal structure of the HmuO, heme oxygenase from Corynebacterium diphtheriae, in complex with azide-bound verdoheme

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-176239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
heme oxygenase (biliverdin-producing) Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 24.17 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54AI1 (Residues: 1-215; Coverage: 100%)
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 106.609Å b: 63.649Å c: 78.52Å
α: 90° β: 130.34° γ: 90°
R-values:
R R work R free
0.182 0.178 0.213
Expression system: Escherichia coli