GL1X · GenesisL1 explorer

Research workbench

Cryo-EM structure of inactive MGLU3 bound to LY341495

Analyse Cryo-EM structure of inactive MGLU3 bound to LY341495 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7WI8
Type
protein
Length
1,446 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Metabotropic glutamate receptor 3
UniProt
Q14832
Ligands
Z99, NAG
Pockets
15 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 33% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMetabotropic glutamate receptor 3protein72333% helix, 10% strandQ14832

Ligands and binding sites

  • Z99 · 2-[(1S,2S)-2-carboxycyclopropyl]-3-(9H-xanthen-9-yl)-D-alanine · ligand · 2 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111190.840.85124empty
210970.840.85123empty
31000.740.9530empty
4620.660.9421empty
5540.630.9314empty

Interfaces

1 interface between chains.

  • A–B · 518 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 7WI8 · Cryo-EM structure of inactive mGlu3 bound to LY341495 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q14832 · AlphaFold monomer V2.0 prediction for metabotropic glutamate receptor 3 (Q14832) · a predicted model of the same protein · chain B against A, TM-score 0.82

Analyse

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