› 4gpf

X-ray diffraction
1.9Å resolution

Structure of the Fe3+-biliverdin-HmuO, heme oxygenase from Corynebacterium diphtheriae (data set III)

Released:
DOI: 10.2210/pdb4gpf/pdb
PDB entry 4gpf coloured by chain, front view.
PDB entry 4gpf coloured by chain, side view.
PDB entry 4gpf coloured by chain, top view.
Source organism: Corynebacterium diphtheriae
Entry authors: Unno M, Ikeda-Saito M

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
heme oxygenase (biliverdin-producing) 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: Q54AI1 (Residues: 1-215; Coverage: 100%)
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

3 bound ligands:
Ligand BLA 3 x BLA
Ligand FE 1 x FE
Ligand SO4 12 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 53.937Å b: 62.539Å c: 107.589Å
α: 90° β: 101.09° γ: 90°
R-values:
R R work R free
0.19 0.185 0.239
Expression system: Escherichia coli

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