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Cryo-EM structure of GLUA2/3 AMPA receptor heterotetramer (model I)

Analyse Cryo-EM structure of GLUA2/3 AMPA receptor heterotetramer (model I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IDE
Type: protein
Length: 2,937 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamate receptor 2; Glutamate receptor 3
UniProt: P19491, P19492
Pockets: 20 · best druggability 0.70

Structure

electron microscopy · 3 distinct chains · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamate receptor 2	protein	735	43% helix, 18% strand	P19491
B, D	Glutamate receptor 3	protein	732	43% helix, 18% strand	P19492
C	Glutamate receptor 2	protein	738	43% helix, 18% strand	P19491

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	832	0.70	0.77	115	empty
2	695	0.69	0.78	90	empty
3	607	0.67	0.78	69	empty
4	879	0.67	0.75	85	empty
5	614	0.67	0.78	107	empty

Interfaces

5 interfaces between chains.

B–C · 439 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 424 Å² buried · 1 hydrogen bond · protein-protein
A–B · 391 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 354 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 23 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5IDE · Cryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model I) · the same entry in another collection · chain A against A, TM-score 1.00
P19492 · AlphaFold monomer V2.0 prediction for glutamate receptor 3 (P19492) · a predicted model of the same protein · chain B against A, TM-score 0.57

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 P19492
Elsewhere: RCSB PDB 5IDE · PDBe 5IDE · UniProt P19491 · UniProt P19492

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