› 3b6h

X-ray diffraction
1.62Å resolution

Crystal structure of human prostacyclin synthase in complex with inhibitor minoxidil

Released:
DOI: 10.2210/pdb3b6h/pdb
PDB entry 3b6h coloured by chain, front view.
PDB entry 3b6h coloured by chain, side view.
PDB entry 3b6h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of prostacyclin synthase and its complexes with substrate analog and inhibitor reveal a ligand-specific heme conformation change.
Li YC, Chiang CW, Yeh HC, Hsu PY, Whitby FG, Wang LH, Chan NL
J Biol Chem 283 2917-26 (2008)
PMID: 18032380

Function and Biology Details

Reactions catalysed: 
A hydroperoxy icosatetraenoate = an oxoicosatetraenoate + H(2)O
(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-6,9-alpha-epoxy-11-alpha,15-dihydroxyprosta-5,13-dienoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172539 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostacyclin synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 498 amino acids
Theoretical weight: 57.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16647 (Residues: 18-500; Coverage: 97%)
Gene names: CYP8, CYP8A1, PTGIS
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand BOG 2 x BOG
Ligand MXD 2 x MXD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P21
Unit cell:
a: 68.762Å b: 106.072Å c: 73.901Å
α: 90° β: 91.81° γ: 90°
R-values:
R R work R free
0.209 0.203 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

10 mentions without citation

Human cytochrome P450 enzymes 5-51 as targets of drugs and natural and environmental compounds: mechanisms, induction, and inhibition - toxic effects and benefits.
Rendic et al. (2018)
9 more