Open state GLUA2 in complex with stz and blocked by agtx-636, after micelle signal subtraction

Structure

electron microscopy · 2 distinct chains · 42% helix, 15% strand (DSSP).

Ligands and binding sites

• GLU · Glutamic acid · ligand · 4 copies · chains A, B, C, D
• CYZ · Cyclothiazide · ligand · 4 copies · chains A, D, B, C
• LU7 · N~1~-{5-[(3-{[3-(L-arginylamino)propyl]amino}propyl)amino]pentyl}-N~2~-[(2,4-dihydroxyphenyl)acetyl]-L-aspartamide · ligand · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• C–D · 4326 Ų buried · 18 hydrogen bonds · protein-protein
• A–B · 4320 Ų buried · 18 hydrogen bonds · protein-protein
• A–D · 3198 Ų buried · 8 hydrogen bonds · protein-protein
• B–C · 3198 Ų buried · 9 hydrogen bonds · protein-protein
• B–D · 394 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

• 6O9G · Open state GluA2 in complex with STZ and blocked by AgTx-636, after micelle signal… · the same entry in another collection · chain D against D, 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 0.71
• Q9Y698 · AlphaFold monomer V2.0 prediction for voltage-dependent calcium channel gamma-2 subunit… · a predicted model of the same protein · chain A against A, TM-score 0.19

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
• Every structure of UniProt Q9Y698
• Elsewhere: RCSB PDB 6O9G · PDBe 6O9G · UniProt P19491 · UniProt Q9Y698