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Cryo-EM structure of GLUN1B-2B nmdar in complex with FAB5 in non- ACTIVE1 conformation

Analyse Cryo-EM structure of GLUN1B-2B nmdar in complex with FAB5 in non- ACTIVE1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TES
Type
protein
Length
3,986 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; FAB5 heavy…
UniProt
P35439, Q00960
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 4 distinct chains · 29% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CGlutamate receptor ionotropic, NMDA 1protein78936% helix, 13% strandP35439
B, DGlutamate receptor ionotropic, NMDA 2Bprotein77436% helix, 15% strandQ00960
H, MFAB5 heavy chainprotein2151% helix, 41% strand—
L, NFAB5 light chainprotein2154% helix, 42% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111480.880.89131empty
22640.840.9549empty
39810.830.84115empty
46090.830.8760empty
52210.830.9531empty

Interfaces

13 interfaces between chains.

  • A–B · 3184 Ų buried · 24 hydrogen bonds · protein-protein
  • C–D · 3170 Ų buried · 23 hydrogen bonds · protein-protein
  • B–C · 3012 Ų buried · 22 hydrogen bonds · protein-protein
  • A–D · 2905 Ų buried · 18 hydrogen bonds · protein-protein
  • M–N · 1885 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 7TES · Cryo-EM structure of GluN1b-2B NMDAR in complex with Fab5 in Non-active1 conformation · the same entry in another collection · chain A against A, TM-score 1.00

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