› 3i9u

X-ray diffraction
2.25Å resolution

Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)

Released:
DOI: 10.2210/pdb3i9u/pdb
PDB entry 3i9u coloured by chain, front view.
PDB entry 3i9u coloured by chain, side view.
PDB entry 3i9u coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase.
Matsui T, Iwasaki M, Sugiyama R, Unno M, Ikeda-Saito M
Inorg Chem 49 3602-9 (2010)
PMID: 20380462

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 30.3 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06762 (Residues: 1-261; Coverage: 90%)
Gene name: Hmox1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand DTU 1 x DTU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3221
Unit cell:
a: 65.882Å b: 65.882Å c: 120.244Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.167 0.223
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
7 more

1 mention without citation

Structural analysis of Cytochrome P450 BM3 mutant M11 in complex with dithiothreitol.
Frydenvang et al. (2019)