› 6n69

X-ray diffraction
2Å 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-128695 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hematopoietic prostaglandin D synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 23.61 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O35543 (Residues: 1-199; Coverage: 100%)
Gene names: Gsts, Hpgds, Pgds, Ptgds2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
1 bound ligand:
Ligand KDV 2 x KDV
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E+
Spacegroup: P212121
Unit cell:
a: 57.188Å b: 80.997Å c: 97.603Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Fragment-based drug discovery: opportunities for organic synthesis.
St Denis et al. (2020)
2 other articles

1 mention without citation

Cryo-EM structure of the folded-back state of human β-cardiac myosin.
Grinzato et al. (2023)

PDB-REDO

The sliders below show the change in model quality between original PDB entry and the PDB-REDO entry

Model Geometry
 
 
Data not available
DNA/RNA Geometry
 
 
Data not available
Fit model/data
 
 
Data not available
PDB-REDO