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MolNFT v1 · #188160 · protein

Cryo-EM structure of GLUN1B-2B nmdar complexed to FAB2 non-ACTIVE2- like

7TEE · Glutamate receptor ionotropic, NMDA 1: “Cryo-EM structure of GLUN1B-2B nmdar complexed to FAB2 non-ACTIVE2- like”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #188160 on GenesisL1: 3D structure, binding sites…

PDB
7TEE
Type
protein
Length
3,567 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate receptor ionotropic, NMDA 1; Glutamate receptor ionotropic, NMDA 2B; FAB2 heavy…
UniProt
P35439, Q00960
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 5 distinct chains · 27% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CGlutamate receptor ionotropic, NMDA 1protein79032% helix, 13% strandP35439
B, DGlutamate receptor ionotropic, NMDA 2Bprotein77134% helix, 11% strandQ00960
HFAB2 heavy chainprotein1170% helix, 37% strand—
L, NFAB2 light chainprotein1060% helix, 38% strand—
MFAB2 heavy chainprotein1160% helix, 35% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111990.870.88121empty
27140.860.9099empty
35940.850.9073empty
44240.840.9262empty
55700.840.8972empty

Interfaces

11 interfaces between chains.

  • C–D · 3221 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 3189 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 2839 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 2795 Ų buried · 9 hydrogen bonds · protein-protein
  • M–N · 1268 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

  • 7TEE · Cryo-EM structure of GluN1b-2B NMDAR complexed to Fab2 Non-active2-like · the same entry in another collection · chain A against A, TM-score 1.00

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