› 1n3u

X-ray diffraction
2.58Å resolution

Crystal structure of human heme oxygenase 1 (HO-1) in complex with its substrate heme, crystal form B

Released:
DOI: 10.2210/pdb1n3u/pdb
PDB entry 1n3u coloured by chain, front view.
PDB entry 1n3u coloured by chain, side view.
PDB entry 1n3u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1.
Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, Ortiz de Montellano PR, Poulos TL
J Biol Chem 278 7834-43 (2003)
PMID: 12500973

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 CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 54.395Å b: 55.92Å c: 79.379Å
α: 90° β: 101.2° γ: 90°
R-values:
R R work R free
0.227 0.225 0.265
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications.
Ryter et al. (2006)
13 more

12 mentions without citation

From Host Heme To Iron: The Expanding Spectrum of Heme Degrading Enzymes Used by Pathogenic Bacteria.
Lyles et al. (2018)
11 more