Open state GLUA2 in complex with stz and blocked by iem-1460, 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
• GZD · N,N,N-trimethyl-5-({[(3S,5S,7S)-tricyclo[3.3.1.1~3, 7~]decan-1-yl]methyl}amino)pentan-1-aminium · 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 · 4370 Ų buried · 19 hydrogen bonds · protein-protein
• A–B · 4356 Ų buried · 19 hydrogen bonds · protein-protein
• B–C · 3204 Ų buried · 7 hydrogen bonds · protein-protein
• A–D · 3201 Ų buried · 8 hydrogen bonds · protein-protein
• B–D · 393 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

• 6DM0 · Open state GluA2 in complex with STZ and blocked by IEM-1460, after micelle signal… · the same entry in another collection · chain A against A, 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 6DM0 · PDBe 6DM0 · UniProt P19491 · UniProt Q9Y698