1iw1

X-ray diffraction
1.5Å resolution

Crystal structure of a heme oxygenase (HmuO) from Corynebacterium diphtheriae complexed with heme in the ferrous state

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-159780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Heme oxygenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 215 amino acids
Theoretical weight: 24.17 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P71119 (Residues: 1-215; Coverage: 100%)
Gene names: DIP1669, hmuO
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 3 x HEM
Carbohydrate polymer : NEW Components: GLC, FRU
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45PX
Spacegroup: P21
Unit cell:
a: 53.865Å b: 62.837Å c: 107.208Å
α: 90° β: 101.02° γ: 90°
R-values:
R R work R free
0.178 0.177 0.202
Expression system: Escherichia coli BL21(DE3)