X-ray structure of IGLUR4 flip ligand-binding core (S1S2) in complex with (S)-AMPA at 1.90A resolution

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 22% strand (DSSP).

Ligands and binding sites

• AMQ · (S)-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid · ligand · 3 copies · chains A, B, C
• SO4 · Sulfate ion · ion · 7 copies · chains A, C, B
• GOL · Glycerol · additive · 9 copies · chains A, C, B
• ACY · Acetic acid · additive · 6 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 895 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 764 Ų buried · 6 hydrogen bonds · protein-protein
• A–C · 264 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

• 3FAT · X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-AMPA at… · the same entry in another collection · chain A against A, TM-score 1.00
• P19493 · AlphaFold monomer V2.0 prediction for glutamate receptor 4 (P19493) · a predicted model of the same protein · chain B against A, TM-score 0.93

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 P19493
• Elsewhere: RCSB PDB 3FAT · PDBe 3FAT · UniProt P19493