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› 2zvu

X-ray diffraction
2.2Å resolution

Crystal structure of rat heme oxygenase-1 in complex with ferrous verdoheme

Released:
DOI: 10.2210/pdb2zvu/pdb
Model geometry
Fit model/data
PDB entry 2zvu coloured by chain, front view.
PDB entry 2zvu coloured by chain, side view.
PDB entry 2zvu coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of rat haem oxygenase-1 in complex with ferrous verdohaem: presence of a hydrogen-bond network on the distal side.
Sato H, Sugishima M, Sakamoto H, Higashimoto Y, Shimokawa C, Fukuyama K, Palmer G, Noguchi M
Biochem J 419 339-45 (2009)
PMID: 19154182

Function and Biology Details

Reaction catalysed: 
heme b + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = biliverdinIXalpha + CO + Fe(2+) + 3 oxidized [NADPH--hemoprotein reductase] + 3 H2O+ H(+).
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: 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 VEA 1 x VEA
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P3221
Unit cell:
a: 65.346Å b: 65.346Å c: 120.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.189 0.24
Expression system: Escherichia coli

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Citations

2 review citations

Heme oxygenation and the widening paradigm of heme degradation.
Wilks et al. (2014)
1 more