› 1vgi

X-ray diffraction
1.9Å resolution

Crystal structure of xenon bound rat heme-heme oxygenase-1 complex

Released:
DOI: 10.2210/pdb1vgi/pdb
PDB entry 1vgi coloured by chain, front view.
PDB entry 1vgi coloured by chain, side view.
PDB entry 1vgi coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
CO-trapping site in heme oxygenase revealed by photolysis of its co-bound heme complex: mechanism of escaping from product inhibition.
Sugishima M, Sakamoto H, Noguchi M, Fukuyama K
J Mol Biol 341 7-13 (2004)
PMID: 15312758

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


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand XE 1 x XE
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P3221
Unit cell:
a: 65.1Å b: 65.1Å c: 120.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.201 0.217
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

1 mention without citation

Electrostatic environment of hemes in proteins: pK(a)s of hydroxyl ligands.
Song et al. (2006)