› 1ozw

X-ray diffraction
1.55Å resolution

Crystal Structures of the Ferric, Ferrous and Ferrous-NO Forms of the Asp140Ala Mutant of Human Heme Oxygenase-1: Catalytic Implications

Released:
DOI: 10.2210/pdb1ozw/pdb
PDB entry 1ozw coloured by chain, front view.
PDB entry 1ozw coloured by chain, side view.
PDB entry 1ozw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications.
Lad L, Wang J, Li H, Friedman J, Bhaskar B, Ortiz de Montellano PR, Poulos TL
J Mol Biol 330 527-38 (2003)
PMID: 12842469

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140705 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 1 soluble form Chains: A, B
Molecule details ›
Chains: A, B
Length: 233 amino acids
Theoretical weight: 26.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09601 (Residues: 1-233; Coverage: 81%)
Gene names: HMOX1, HO, HO1
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 61.681Å b: 54.5Å c: 70.921Å
α: 90° β: 98.81° γ: 90°
R-values:
R R work R free
0.212 0.212 0.237
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structure and catalytic mechanism of heme oxygenase.
Unno et al. (2007)
3 more

1 mention without citation

Alteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding network.
Wang et al. (2006)