PDBe 1wnw

X-ray diffraction
1.7Å resolution

D136N mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)

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
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: P71119 (Residues: 1-215; Coverage: 100%)
Gene names: DIP1669, hmuO
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 54.059Å b: 63.101Å c: 107.164Å
α: 90° β: 101.03° γ: 90°
R-values:
R R work R free
0.199 0.196 0.233
Expression system: Escherichia coli