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Crystal Structures of mPGES-1 Inhibitor Complexes
Analyse Crystal Structures of mPGES-1 Inhibitor Complexes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YL0
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.52
- Source
- Homo sapiens
- Molecule
- Prostaglandin E synthase
- EC
- 5.3.99.3
- UniProt
- O14684
- Ligands
- 4DZ, GSH
Structure
x-ray diffraction · resolution 1.52 · 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
- 4DZ · 2-(9-chloro-1H-phenanthro[9,10-d]imidazol-2-yl)benzene-1,3-dicarbonitrile · ligand · chains A
- GSH · Glutathione · ligand · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A
- PG4 · Tetraethylene glycol · 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 4YL0 · PDBe 4YL0 · UniProt O14684
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