› 3k4f

X-ray diffraction
2.17Å resolution

X-Ray Crystal Structure of Human Heme Oxygenase-1 in Complex with 4-Phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone

Released:
DOI: 10.2210/pdb3k4f/pdb
PDB entry 3k4f coloured by chain, front view.
PDB entry 3k4f coloured by chain, side view.
PDB entry 3k4f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Heme oxygenase inhibition by 2-oxy-substituted 1-azolyl-4-phenylbutanes: effect of variation of the azole moiety. X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone.
Roman G, Rahman MN, Vukomanovic D, Jia Z, Nakatsu K, Szarek WA
Chem Biol Drug Des 75 68-90 (2010)
PMID: 19954435

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:
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
3 bound ligands:
Ligand Q86 2 x Q86
Ligand HEZ 2 x HEZ
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21
Unit cell:
a: 52.205Å b: 52.483Å c: 73.977Å
α: 90° β: 90.21° γ: 90°
R-values:
R R work R free
0.225 0.222 0.28
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Novel Structural Insight into Inhibitors of Heme Oxygenase-1 (HO-1) by New Imidazole-Based Compounds: Biochemical and In Vitro Anticancer Activity Evaluation.
Greish et al. (2018)
12 more

2 mentions without citation

Structural insights into human heme oxygenase-1 inhibition by potent and selective azole-based compounds.
Rahman et al. (2013)
1 more