GL1X · GenesisL1 explorer

MolNFT v1 · #122037 · protein

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

5IDE · Glutamate receptor 2: “Cryo-EM structure of GLUA2/3 AMPA receptor heterotetramer (model I)”. Electron microscopy, 20 pockets (best druggability 0.70). MolNFT v1 #122037 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate receptor 2protein73543% helix, 18% strandP19491
B, DGlutamate receptor 3protein73243% helix, 18% strandP19492
CGlutamate receptor 2protein73843% helix, 18% strandP19491

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18320.700.77115empty
26950.690.7890empty
36070.670.7869empty
48790.670.7585empty
56140.670.78107empty

Interfaces

5 interfaces between chains.

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

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