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MolNFT v1 · #158842 · protein

Structure of the TRPM8 cold receptor by single particle electron cryo- microscopy, ligand-free state

6O6A · Transient receptor potential cation channel subfamily M…: “Structure of the TRPM8 cold receptor by single particle electron cryo- microscopy, ligand-free state”. Electron microscopy, 2 ligands (Y01, NA), 20 pockets (best…

PDB
6O6A
Type
protein
Length
3,312 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transient receptor potential cation channel subfamily M member 8
Ligands
Y01, NA
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 57% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DTransient receptor potential cation channel subfamily M member 8protein82857% helix, 4% strand—

Ligands and binding sites

  • Y01 · Cholesterol hemisuccinate · ligand · 4 copies · chains A, B, C, D
  • NA · Sodium ion · metal · 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, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11330.800.9622empty
27260.790.8368Y01
37750.790.8282Y01
48180.790.8271Y01
57880.780.8278Y01

Interfaces

6 interfaces between chains.

  • A–B · 4285 Ų buried · 29 hydrogen bonds · protein-protein
  • A–D · 4256 Ų buried · 29 hydrogen bonds · protein-protein
  • B–C · 4250 Ų buried · 29 hydrogen bonds · protein-protein
  • C–D · 4196 Ų buried · 31 hydrogen bonds · protein-protein
  • B–D · 69 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6O6A · Structure of the TRPM8 cold receptor by single particle electron cryo-microscopy… · the same entry in another collection · chain A against A, TM-score 1.00

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