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Crystal structure of the GLUK2/GLUK5 (GLUR6/KA2) atd tetramer assembly

Analyse Crystal structure of the GLUK2/GLUK5 (GLUR6/KA2) atd tetramer assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QLV
Type
protein
Length
3,760 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate receptor, ionotropic kainate 5; Glutamate receptor, ionotropic kainate 2
UniProt
Q63273, P42260
Pockets
20 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, E, G, IGlutamate receptor, ionotropic kainate 5protein37133% helix, 18% strandQ63273
C, D, F, H, JGlutamate receptor, ionotropic kainate 2protein38133% helix, 17% strandP42260

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19780.810.82106empty
211780.800.81120empty
311710.800.81112empty
411450.800.81109empty
55790.750.8268empty

Interfaces

9 interfaces between chains.

  • E–F · 1707 Ų buried · 23 hydrogen bonds · protein-protein
  • G–H · 1665 Ų buried · 21 hydrogen bonds · protein-protein
  • A–C · 1662 Ų buried · 20 hydrogen bonds · protein-protein
  • B–D · 1616 Ų buried · 17 hydrogen bonds · protein-protein
  • I–J · 1560 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

  • 3QLV · Crystal structure of the GluK2/GluK5 (GluR6/KA2) ATD tetramer assembly · the same entry in another collection · chain J against J, TM-score 1.00
  • Q63273 · AlphaFold monomer V2.0 prediction for glutamate receptor ionotropic, kainate 5 (Q63273) · a predicted model of the same protein · chain A against A, TM-score 0.96

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