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Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y- N754S) in complex with glutamate and me-CX516 at 1.72 a resolution

Analyse Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y- N754S) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IY6
Type
protein
Length
263 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate receptor 2
UniProt
P19491
Ligands
MQS, MQR, GLU, SO4
Pockets
2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate receptor 2protein26338% helix, 21% strandP19491

Ligands and binding sites

  • MQS · [(3S)-3-methylpiperidin-1-yl](quinoxalin-6-yl)methanone · ligand · 2 copies · chains A
  • MQR · [(3R)-3-methylpiperidin-1-yl](quinoxalin-6-yl)methanone · ligand · chains A
  • GLU · Glutamic acid · ligand · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.430.7624SO4
2620.350.7720empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4IY6 · Crystal structure of the GLUA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P19491 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P19491) · a predicted model of the same protein · chain A against A, TM-score 0.97

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