› 1xk2

X-ray diffraction
2.2Å resolution

NADPH- and Ascorbate-Supported Heme Oxygenase Reactions are Distinct. Regiospecificity of Heme Cleavage by the R183E Mutant

Released:
DOI: 10.2210/pdb1xk2/pdb
PDB entry 1xk2 coloured by chain, front view.
PDB entry 1xk2 coloured by chain, side view.
PDB entry 1xk2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant.
Wang J, Lad L, Poulos TL, Ortiz de Montellano PR
J Biol Chem 280 2797-806 (2005)
PMID: 15525643

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: 26.87 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
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 61.371Å b: 54.712Å c: 71.889Å
α: 90° β: 99.13° γ: 90°
R-values:
R R work R free
0.22 0.22 0.23
Expression system: Escherichia coli

Quick links

Citations

5 review citations

New insights into intracellular locations and functions of heme oxygenase-1.
Dunn et al. (2014)
4 more