› 7jr8

X-ray diffraction
1.13Å resolution

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 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
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 23.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60760 (Residues: 1-199; Coverage: 100%)
Gene names: GSTS, HPGDS, PGDS, PTGDS2
Sequence domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
5 bound ligands:
Ligand CL 1 x CL
Ligand EDO 3 x EDO
Ligand VH7 2 x VH7
Ligand MG 2 x MG
Ligand NA 3 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 47.082Å b: 93.489Å c: 47.913Å
α: 90° β: 105.519° γ: 90°
R-values:
R R work R free
0.115 0.115 0.143
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

5-Nitrofuran-Tagged Oxazolyl Pyrazolopiperidines: Synthesis and Activity against ESKAPE Pathogens.
Rogacheva et al. (2023)

1 mention without citation

Hidden Glutathione Transferases in the Human Genome.
Oakley AJ. (2023)