› 2cvd

X-ray diffraction
1.45Å resolution

Crystal structure analysis of human hematopoietic prostaglandin D synthase complexed with HQL-79

Released:
DOI: 10.2210/pdb2cvd/pdb
PDB entry 2cvd coloured by chain, front view.
PDB entry 2cvd coloured by chain, side view.
PDB entry 2cvd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional characterization of HQL-79, an orally selective inhibitor of human hematopoietic prostaglandin D synthase.
Aritake K, Kado Y, Inoue T, Miyano M, Urade Y
J Biol Chem 281 15277-86 (2006)
PMID: 16547010

Function and Biology Details

Reactions catalysed: 
RX + glutathione = HX + R-S-glutathione
(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hematopoietic prostaglandin D synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 198 amino acids
Theoretical weight: 23.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60760 (Residues: 2-199; Coverage: 100%)
Gene names: GSTS, HPGDS, PGDS, PTGDS2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 4 x GSH
3 bound ligands:
Ligand MG 2 x MG
Ligand HQL 4 x HQL
Ligand GOL 7 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P1
Unit cell:
a: 46.937Å b: 49.085Å c: 93.137Å
α: 85.83° β: 88.71° γ: 89.98°
R-values:
R R work R free
0.192 0.192 0.209
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Glutathione transferases, regulators of cellular metabolism and physiology.
Board et al. (2013)
9 more

7 mentions without citation

Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis.
Smith et al. (2011)
6 more