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Structure of squirrel TRPV1 in apo state

Analyse Structure of squirrel TRPV1 in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LQY
Type
protein
Length
2,636 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Osm-9-like TRP channel 1
UniProt
I3LZN5
Ligands
POV, YBG, NA, CL
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 51% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DOsm-9-like TRP channel 1protein65951% helix, 4% strandI3LZN5

Ligands and binding sites

  • POV · (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate · ligand · 32 copies · chains A, B, D, C
  • YBG · 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoinositol · ligand · 4 copies · chains A, B, C, D
  • NA · Sodium ion · metal · chains A, B, C, D
  • CL · Chloride ion · ion · 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, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110710.820.8398empty
21500.820.9820empty
37510.810.8571YBG, POV
49420.810.8281YBG, POV
510100.800.8184YBG, POV

Interfaces

6 interfaces between chains.

  • C–D · 3420 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 3419 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 3418 Ų buried · 20 hydrogen bonds · protein-protein
  • A–D · 3418 Ų buried · 18 hydrogen bonds · protein-protein
  • B–D · 48 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7LQY · Structure of squirrel TRPV1 in apo state · the same entry in another collection · chain A against A, TM-score 1.00

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