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Crystal structure of the ankyrin repeat domain of TRPV2

Analyse Crystal structure of the ankyrin repeat domain of TRPV2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ETB
Type
protein
Length
252 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transient receptor potential cation channel subfamily V member 2
UniProt
Q9WUD2
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransient receptor potential cation channel subfamily V member 2protein25254% helix, 2% strandQ9WUD2

Ligands and binding sites

  • ACY · Acetic acid · additive · 4 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11140.400.7618empty
2500.290.7511empty

Compared structures

  • 2ETB · Crystal structure of the ankyrin repeat domain of TRPV2 · 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 0.97

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