› 2q32

X-ray diffraction
2.4Å resolution

Crystal structure of human heme oxygenase-2 C127A (HO-2)

Released:
DOI: 10.2210/pdb2q32/pdb
PDB entry 2q32 coloured by chain, front view.
PDB entry 2q32 coloured by chain, side view.
PDB entry 2q32 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2.
Bianchetti CM, Yi L, Ragsdale SW, Phillips GN
J Biol Chem 282 37624-31 (2007)
PMID: 17965015

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 2 soluble form Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 30.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30519 (Residues: 1-264; Coverage: 84%)
Gene names: HMOX2, HO2
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

1 bound ligand:
Ligand OXN 2 x OXN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 75.769Å b: 86.017Å c: 97.753Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
10 more

87 mentions without citation

Sp1- and Krüppel-like transcription factors.
Kaczynski et al. (2003)
86 more