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Structure of human TRPV3 in the presence of 2-apb in C4 symmetry

Analyse Structure of human TRPV3 in the presence of 2-apb in C4 symmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MHV
Type
protein
Length
2,452 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transient receptor potential cation channel subfamily V member 3
UniProt
Q8NET8
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 58% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, C, A, DTransient receptor potential cation channel subfamily V member 3protein61358% helix, 5% strandQ8NET8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111590.850.8588empty
28300.780.81117empty
34800.700.8047empty
43380.700.8228empty
53370.700.8231empty

Interfaces

6 interfaces between chains.

  • A–D · 2708 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 2706 Ų buried · 13 hydrogen bonds · protein-protein
  • B–A · 2699 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 2685 Ų buried · 13 hydrogen bonds · protein-protein
  • C–A · 14 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6MHV · Structure of human TRPV3 in the presence of 2-APB in C4 symmetry · the same entry in another collection · chain B against B, TM-score 1.00
  • Q8NET8 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain B against A, TM-score 0.98

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