Crystal structure of the GLUA2 ligand-binding domain (S1S2J) in complex with glutamate and positive allosteric modulator BPAM538

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

Ligands and binding sites

• GLU · Glutamic acid · ligand · 3 copies · chains A, B, C
• 9TE · 4-cyclopropyl-7-(3-methoxyphenoxy)-2,3-dihydro-1$L^{6}, 2,4-benzothiadiazine 1,1-dioxide · ligand · 2 copies · chains A, B, C
• ZN · Zinc ion · metal · 17 copies · chains A, C, B
• ACT · Acetate ion · additive · 4 copies · chains A, B, C

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• A–B · 988 Ų buried · 11 hydrogen bonds · protein-protein
• A–C · 314 Ų buried · 8 hydrogen bonds · protein-protein
• B–C · 94 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

• 5OEW · Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with glutamate… · the same entry in another collection · chain B against B, TM-score 1.00
• P19491 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P19491) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P19491
• Elsewhere: RCSB PDB 5OEW · PDBe 5OEW · UniProt P19491