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Activated state of 2-apb and cbd-bound wildtype rat TRPV2 in nanodiscs

Analyse Activated state of 2-apb and cbd-bound wildtype rat TRPV2 in nanodiscs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7T37
Type
protein
Length
2,476 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transient receptor potential cation channel subfamily V member 2
UniProt
Q9WUD2
Ligands
P0T, FZ4
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 55% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DTransient receptor potential cation channel subfamily V member 2protein61955% helix, 6% strandQ9WUD2

Ligands and binding sites

  • P0T · cannabidiol · ligand · 4 copies · chains A, B, C, D
  • FZ4 · 2-aminoethyl diphenylborinate · ligand · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18550.850.8684P0T
23370.800.9029empty
33230.790.9028empty
46170.790.8461empty
53180.790.8932empty

Interfaces

4 interfaces between chains.

  • B–C · 2807 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 2804 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 2803 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 2799 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 7T37 · Activated state of 2-APB and CBD-bound wildtype rat TRPV2 in nanodiscs · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WUD2 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

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