5uca

X-ray diffraction
2.12Å resolution

Crystal structure of human Heme Oxygenase-2 in complex with Laurate

Released:
Source organism: Homo sapiens
Primary publication:
Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling.
Cell Host Microbe 21 220-230 (2017)
PMID: 28132836

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-151751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heme oxygenase 2 soluble form Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 226 amino acids
Theoretical weight: 26.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30519 (Residues: 30-242; Coverage: 67%)
Gene names: HMOX2, HO2
Sequence domains: Heme oxygenase
Structure domains: Heme oxygenase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 77.363Å b: 83.92Å c: 138.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.249
Expression system: Escherichia coli