› 1j2c

X-ray diffraction
2.4Å resolution

Crystal structure of rat heme oxygenase-1 in complex with biliverdin IXalpha-iron cluster

Released:
DOI: 10.2210/pdb1j2c/pdb
PDB entry 1j2c coloured by chain, front view.
PDB entry 1j2c coloured by chain, side view.
PDB entry 1j2c coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate. Conformational change of the distal helix during the heme cleavage reaction.
Sugishima M, Sakamoto H, Higashimoto Y, Noguchi M, Fukuyama K
J Biol Chem 278 32352-8 (2003)
PMID: 12794075

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 domain:

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: 267 amino acids
Theoretical weight: 30.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06762 (Residues: 1-267; Coverage: 92%)
Gene name: Hmox1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand BLA 1 x BLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P3221
Unit cell:
a: 65.4Å b: 65.4Å c: 121.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.194 0.239
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Heme oxygenase and heme degradation.
Kikuchi et al. (2005)
3 more

2 mentions without citation

SitesIdentify: a protein functional site prediction tool.
Bray et al. (2009)
1 more