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Crystal structure of the GLUR2 ligand binding domain mutant (S1S2J- N754D) in complex with kainate at 2.1 a resolution

Analyse Crystal structure of the GLUR2 ligand binding domain mutant (S1S2J- N754D) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LBB
Type
protein
Length
258 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamine receptor 2
UniProt
P19491
Ligands
KAI
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamine receptor 2protein25838% helix, 22% strandP19491

Ligands and binding sites

  • KAI · 3-(carboxymethyl)-4-isopropenylproline · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12650.650.8239KAI

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1LBB · Crystal structure of the GluR2 ligand binding domain mutant (S1S2J-N754D) 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 0.99

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