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Cryo-EM structure of full-length TRPV1 at PH6B state

Analyse Cryo-EM structure of full-length TRPV1 at PH6B state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7L2K
Type
protein
Length
1,976 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transient receptor potential cation channel subfamily V member 1
UniProt
O35433
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 61% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, D, BTransient receptor potential cation channel subfamily V member 1protein49461% helix, 2% strandO35433

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12930.850.9535empty
210480.820.82101empty
310610.810.8296empty
410340.810.8283empty
56090.770.8354empty

Interfaces

6 interfaces between chains.

  • A–D · 2148 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 2138 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 2128 Ų buried · 4 hydrogen bonds · protein-protein
  • C–B · 2056 Ų buried · 5 hydrogen bonds · protein-protein
  • D–B · 33 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7L2K · Cryo-EM structure of full-length TRPV1 at pH6b state · the same entry in another collection · chain A against A, TM-score 1.00
  • O35433 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain A against A, TM-score 0.95

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