› 2iag

X-ray diffraction
2.15Å resolution

Crystal structure of human prostacyclin synthase

Released:
DOI: 10.2210/pdb2iag/pdb
PDB entry 2iag coloured by chain, front view.
PDB entry 2iag coloured by chain, side view.
PDB entry 2iag coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human prostacyclin synthase.
Chiang CW, Yeh HC, Wang LH, Chan NL
J Mol Biol 364 266-74 (2006)
PMID: 17020766

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: 482 amino acids
Theoretical weight: 55.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16647 (Residues: 23-500; Coverage: 96%)
Gene names: CYP8, CYP8A1, PTGIS
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1, SPRING-8 BEAMLINE BL12B2
Spacegroup: P21
Unit cell:
a: 67.733Å b: 105.596Å c: 73.95Å
α: 90° β: 92.01° γ: 90°
R-values:
R R work R free
0.204 0.201 0.263
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

19 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)
18 more