Cryo-EM structure of thermo-sensitive TRP channel TRP1 from the alga chlamydomonas reinhardtii in detergent

Structure

electron microscopy · 2 distinct chains · 55% helix, 0% strand (DSSP).

Ligands and binding sites

• PIK · (2S)-3-{[(R)-hydroxy{[(1r,2r,3s,4r,5r,6s)-2,3,6-trihydroxy-4,5-bis(phosphonooxy) cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dihexadecanoate · ligand · 4 copies · chains A, B, C, D
• PIO · [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2, 3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate · ligand · 2 copies · chains A, C
• PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A, D, B, C
• CPL · 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine · ligand · 2 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.

Interfaces

6 interfaces between chains.

• A–D · 4517 Ų buried · 33 hydrogen bonds · protein-protein
• B–C · 4498 Ų buried · 34 hydrogen bonds · protein-protein
• A–B · 4054 Ų buried · 22 hydrogen bonds · protein-protein
• C–D · 4027 Ų buried · 21 hydrogen bonds · protein-protein
• B–D · 260 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent (covalent ligand).

Compared structures

• 6PW4 · Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q0Z852
• Elsewhere: RCSB PDB 6PW4 · PDBe 6PW4 · UniProt Q0Z852