Open-state cryo-EM structure of human TRPV3 in presence of 2-APB in cNW30 nanodiscs. Determined by electron microscopy at 2.59 Å resolution. Released 17 Apr 2024.
Explore 8V6N in 3D Show helices and sheets RCSB PDB PDBe
8V6N contains 140 α-helices and 52 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 73-74 | 2 | 1 |
| α-helix | 119-127 | 9 | |
| α-helix | 132-143 | 12 | |
| α-helix | 154-160 | 7 | |
| β-strand | 163 | 1 | 2 |
| β-strand | 170 | 1 | 2 |
| α-helix | 171-177 | 7 | |
| α-helix | 184-196 | 13 | |
| α-helix | 200-203 | 4 | |
| α-helix | 218-224 | 7 | |
| α-helix | 228-235 | 8 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-305 | 7 | |
| α-helix | 316-328 | 13 | |
| α-helix | 344-351 | 8 | |
| α-helix | 354-361 | 8 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-382 | 7 | 3 |
| β-strand | 385-390 | 6 | 3 |
| α-helix | 403-408 | 6 | |
| α-helix | 416-419 | 4 | |
| α-helix | 425-432 | 8 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-459 | 22 | |
| α-helix | 481-506 | 26 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-560 | 14 | |
| α-helix | 561-566 | 6 | |
| α-helix | 575-582 | 8 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 4 |
| α-helix | 610-613 | 4 | |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 4 |
| α-helix | 651-661 | 11 | |
| α-helix | 662-669 | 8 | |
| α-helix | 670-686 | 17 | |
| α-helix | 688-705 | 18 | |
| α-helix | 709-712 | 4 | |
| β-strand | 720 | 1 | 5 |
| β-strand | 721 | 1 | 6 |
| β-strand | 724 | 1 | 7 |
| β-strand | 727 | 1 | 7 |
| β-strand | 730 | 1 | 5 |
| β-strand | 733-737 | 5 | 3 |
| α-helix | 739-747 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 74 | 1 | 6 |
| α-helix | 119-127 | 9 | |
| α-helix | 132-143 | 12 | |
| α-helix | 154-160 | 7 | |
| β-strand | 163 | 1 | 8 |
| β-strand | 170 | 1 | 8 |
| α-helix | 171-177 | 7 | |
| α-helix | 184-196 | 13 | |
| α-helix | 200-203 | 4 | |
| α-helix | 218-224 | 7 | |
| α-helix | 228-235 | 8 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-305 | 7 | |
| α-helix | 316-328 | 13 | |
| α-helix | 344-351 | 8 | |
| α-helix | 354-361 | 8 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-382 | 7 | 9 |
| β-strand | 385-390 | 6 | 9 |
| α-helix | 403-408 | 6 | |
| α-helix | 416-419 | 4 | |
| α-helix | 425-432 | 8 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-459 | 22 | |
| α-helix | 481-506 | 26 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-560 | 14 | |
| α-helix | 561-566 | 6 | |
| α-helix | 575-582 | 8 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 10 |
| α-helix | 610-613 | 4 | |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 10 |
| α-helix | 651-661 | 11 | |
| α-helix | 662-669 | 8 | |
| α-helix | 670-686 | 17 | |
| α-helix | 688-705 | 18 | |
| α-helix | 709-712 | 4 | |
| β-strand | 720 | 1 | 11 |
| β-strand | 721-722 | 2 | 12 |
| β-strand | 724 | 1 | 13 |
| β-strand | 727 | 1 | 13 |
| β-strand | 730 | 1 | 11 |
| β-strand | 733-737 | 5 | 9 |
| α-helix | 739-747 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 73-74 | 2 | 12 |
| α-helix | 119-127 | 9 | |
| α-helix | 132-143 | 12 | |
| α-helix | 154-160 | 7 | |
| β-strand | 163 | 1 | 14 |
| β-strand | 170 | 1 | 14 |
| α-helix | 171-177 | 7 | |
| α-helix | 184-196 | 13 | |
| α-helix | 200-203 | 4 | |
| α-helix | 218-224 | 7 | |
| α-helix | 228-235 | 8 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-305 | 7 | |
| α-helix | 316-328 | 13 | |
| α-helix | 344-351 | 8 | |
| α-helix | 354-361 | 8 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-382 | 7 | 15 |
| β-strand | 385-390 | 6 | 15 |
| α-helix | 403-408 | 6 | |
| α-helix | 416-419 | 4 | |
| α-helix | 425-432 | 8 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-459 | 22 | |
| α-helix | 481-506 | 26 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-560 | 14 | |
| α-helix | 561-566 | 6 | |
| α-helix | 575-582 | 8 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 16 |
| α-helix | 610-613 | 4 | |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 16 |
| α-helix | 651-661 | 11 | |
| α-helix | 662-669 | 8 | |
| α-helix | 670-686 | 17 | |
| α-helix | 688-705 | 18 | |
| α-helix | 709-712 | 4 | |
| β-strand | 720 | 1 | 17 |
| β-strand | 721-722 | 2 | 18 |
| β-strand | 724 | 1 | 19 |
| β-strand | 727 | 1 | 19 |
| β-strand | 730 | 1 | 17 |
| β-strand | 733-737 | 5 | 15 |
| α-helix | 739-747 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 3 | A, B, C, D | protein | 808 | Homo sapiens | Q8NET8 (AlphaFold model) |
>8V6N_1 Transient receptor potential cation channel subfamily V member 3 (chains A, B, C, D) MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTS PPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLK KRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNIN PNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGAD VNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNIL HALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYI LSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEML TLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMG WLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLY LFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLG FGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLIT YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGEL CKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTADFNKIQDSSRNNSKTTLNAF EEVEEFPETSVLVPRGSAAAWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| FZ4 | 2-aminoethyl diphenylborinate | C14 H16 B N O | 8 |
| ACD | Arachidonic acid | C20 H32 O2 | 4 |
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 20 |
Water and common crystallization additives (NA) are not listed.
TRPV3 activation by different agonists accompanied by lipid dissociation from the vanilloid site. Nadezhdin, K.D., Neuberger, A., Khosrof, L.S. et al. Sci Adv (2024) 10:eadn2453-eadn2453. DOI 10.1126/sciadv.adn2453 · PubMed
Other PDB entries of the same protein (UniProt Q8NET8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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