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

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

PDB
5IDF
Type
protein
Length
2,947 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 0.68

Structure

electron microscopy · 4 distinct chains · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate receptor 2protein74143% helix, 18% strandP19491
BGlutamate receptor 3protein73443% helix, 18% strandP19492
CGlutamate receptor 2protein73843% helix, 18% strandP19491
DGlutamate receptor 3protein73443% helix, 18% strandP19492

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17200.680.77105empty
29370.680.7583empty
34510.680.8068empty
45940.670.7899empty
55090.670.7992empty

Interfaces

4 interfaces between chains.

  • C–D · 499 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 467 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 315 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 265 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5IDF · Cryo-EM structure of GluA2/3 AMPA receptor heterotetramer (model II) · 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 0.67

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