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Crystal structure of the GLUK5 (KA2) atd dimer at 1.7 ångström resolution

Analyse Crystal structure of the GLUK5 (KA2) atd dimer at 1.7 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OM1
Type
protein
Length
740 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate receptor ionotropic, kainate 5
UniProt
Q63273
Ligands
NAG, NA
Pockets
8 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate receptor ionotropic, kainate 5protein37339% helix, 20% strandQ63273
BGlutamate receptor ionotropic, kainate 5protein36739% helix, 20% strandQ63273

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B
  • NA · Sodium ion · metal · 2 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111370.800.81109empty
24910.720.8162NAG
3760.620.9017empty
41240.550.8230empty
51650.530.7922empty

Interfaces

1 interface between chains.

  • A–B · 1287 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 glycan, 5 disulfide (N-glycosylation, disulfide).

Compared structures

  • 3OM1 · Crystal structure of the GluK5 (KA2) ATD dimer at 1.7 Angstrom Resolution · the same entry in another collection · chain A against A, 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 B against A, TM-score 0.98

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