› 4yl3

X-ray diffraction
1.41Å 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)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin E synthase Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.69 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O14684 (Residues: 5-152; Coverage: 97%)
Gene names: MGST1L1, MPGES1, PGES, PIG12, PTGES
Sequence domains: MAPEG family
Structure domains: Membrane associated eicosanoid/glutathione metabolism-like domain

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
3 bound ligands:
Ligand 4U9 1 x 4U9
Ligand BOG 2 x BOG
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: R3
Unit cell:
a: 76.434Å b: 76.434Å c: 123.264Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.166 0.183
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

Breaking barriers to novel analgesic drug development.
Yekkirala et al. (2017)
3 more

5 mentions without citation

A dynamic Asp-Arg interaction is essential for catalysis in microsomal prostaglandin E2 synthase.
Brock et al. (2016)
4 more