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Crystal structure of mpges-1 bound to inhibitor
Analyse Crystal structure of mpges-1 bound to inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TL9
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prostaglandin E synthase
- EC
- 5.3.99.3
- UniProt
- O14684
- Ligands
- 7DN, GSH, JZR
Structure
x-ray diffraction · 1 distinct chain · 80% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostaglandin E synthase (EC 5.3.99.3) | protein | 148 | 80% helix, 1% strand | O14684 |
Ligands and binding sites
- 7DN · 2-{2-[(1S,2S)-2-{[1-(8-methylquinolin-2-yl)piperidine-4-carbonyl]amino}cyclopentyl]ethyl}benzoic acid · ligand · chains A
- GSH · Glutathione · ligand · chains A
- JZR · hexyl beta-D-glucopyranoside · ligand · chains A
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A
- BOG · octyl beta-D-glucopyranoside · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O14684
- Elsewhere: RCSB PDB 5TL9 · PDBe 5TL9 · UniProt O14684
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