GL1X · GenesisL1 explorer

MolNFT v1 · #149107 · protein

GLUA2(FLOP) G724C ligand binding core dimer bound to L-glutamate (form a) at 2.34 ångström resolution

6FQG · Glutamate receptor 2,GLUTAMATE receptor 2: “GLUA2(FLOP) G724C ligand binding core dimer bound to L-glutamate (form a) at 2.34 ångström resolution”. X-ray diffraction, 1 ligand (GGL), 5 pockets (best druggability 0.71). MolNFT v1…

PDB
6FQG
Type
protein
Length
517 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate receptor 2,GLUTAMATE receptor 2
UniProt
P19491
Ligands
GGL
Pockets
5 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate receptor 2,GLUTAMATE receptor 2protein25838% helix, 21% strandP19491
BGlutamate receptor 2,GLUTAMATE receptor 2protein25937% helix, 20% strandP19491

Ligands and binding sites

  • GGL · Gamma-L-glutamic acid · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17120.710.7853empty
21310.460.7819empty
31240.450.7819empty
4940.410.7824empty
51180.390.7528empty

Interfaces

1 interface between chains.

  • A–B · 492 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 6FQG · GluA2(flop) G724C ligand binding core dimer bound to L-Glutamate (Form A) at 2.34… · 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 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.