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Structure of the TRPM8 cold receptor by single particle electron cryo- microscopy, calcium-bound state

Analyse Structure of the TRPM8 cold receptor by single particle electron cryo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O77
Type
protein
Length
3,488 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, CA
Pockets
20 · best druggability 0.84

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DTransient receptor potential cation channel subfamily M member 8protein87258% helix, 5% strand—

Ligands and binding sites

  • Y01 · Cholesterol hemisuccinate · ligand · 12 copies · chains A, D, B, C
  • CA · Calcium 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
110010.840.8576empty
210130.770.7989empty
31050.770.9619empty
49680.770.7990empty
58440.770.8073empty

Interfaces

6 interfaces between chains.

  • A–B · 4237 Ų buried · 31 hydrogen bonds · protein-protein
  • A–D · 4231 Ų buried · 31 hydrogen bonds · protein-protein
  • B–C · 4230 Ų buried · 31 hydrogen bonds · protein-protein
  • C–D · 4228 Ų buried · 31 hydrogen bonds · protein-protein
  • A–C · 21 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 6O77 · 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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