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Glutamate bound to a double cysteine mutant (V484C/E657C) of the ligand binding domain of GLUA2

Analyse Glutamate bound to a double cysteine mutant (V484C/E657C) of the ligand binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3T9X
Type
protein
Length
774 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate receptor 2
UniProt
P19491
Ligands
GLU, ZN
Pockets
7 · best druggability 0.76

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
B, D, FGlutamate receptor 2protein25838% helix, 21% strandP19491

Ligands and binding sites

  • GLU · Glutamic acid · ligand · 3 copies · chains B, D, F
  • ZN · Zinc ion · metal · 5 copies · chains B, D, F

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16550.760.8287empty
23710.620.7842empty
32780.570.7831empty
4990.400.7622empty
5620.380.7916empty

Interfaces

2 interfaces between chains.

  • B–F · 1051 Ų buried · 11 hydrogen bonds · protein-protein
  • D–F · 295 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 3T9X · Glutamate bound to a double cysteine mutant (V484C/E657C) of the ligand binding domain of… · the same entry in another collection · chain B against B, TM-score 1.00
  • P19491 · AlphaFold monomer V2.0 prediction for glutamate receptor 2 (P19491) · a predicted model of the same protein · chain B against A, TM-score 0.98

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