1wzd

X-ray diffraction
1.35Å resolution

Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenase

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-176240 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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 BL21(DE3)
UniProt:
  • Canonical: Q54AI1 (Residues: 1-215; Coverage: 100%)
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

3 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: 41.257Å b: 63.009Å c: 78.159Å
α: 90° β: 98.52° γ: 90°
R-values:
R R work R free
0.176 0.173 0.204
Expression system: Escherichia coli BL21(DE3)