Structure of the human TRPV3 channel in the apo conformation. Determined by electron microscopy at 3.4 Å resolution. Released 3 Oct 2018.
Explore 6MHO in 3D Show helices and sheets RCSB PDB PDBe
6MHO contains 140 α-helices and 24 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 |
|---|---|---|---|
| α-helix | 119-129 | 11 | |
| α-helix | 133-146 | 14 | |
| α-helix | 155-162 | 8 | |
| β-strand | 163-164 | 2 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 171-177 | 7 | |
| α-helix | 183-196 | 14 | |
| α-helix | 200-204 | 5 | |
| α-helix | 218-224 | 7 | |
| α-helix | 228-236 | 9 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-283 | 9 | |
| α-helix | 299-306 | 8 | |
| α-helix | 310-313 | 4 | |
| α-helix | 316-327 | 12 | |
| α-helix | 332-335 | 4 | |
| α-helix | 344-350 | 7 | |
| α-helix | 355-360 | 6 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-378 | 3 | 6 |
| β-strand | 385-391 | 7 | 6 |
| α-helix | 403-409 | 7 | |
| α-helix | 423-432 | 10 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-460 | 23 | |
| α-helix | 481-505 | 25 | |
| α-helix | 521-541 | 21 | |
| α-helix | 547-561 | 15 | |
| α-helix | 562-567 | 6 | |
| α-helix | 571-581 | 11 | |
| α-helix | 582-586 | 5 | |
| α-helix | 587-608 | 22 | |
| α-helix | 609-611 | 3 | |
| α-helix | 625-637 | 13 | |
| α-helix | 641-645 | 5 | |
| α-helix | 651-679 | 29 | |
| α-helix | 680-684 | 5 | |
| α-helix | 685-704 | 20 | |
| α-helix | 709-715 | 7 | |
| β-strand | 719-721 | 3 | 6 |
| β-strand | 729-737 | 9 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 3 | A, B, C, D | protein | 826 | Homo sapiens | Q8NET8 (AlphaFold model) |
>6MHO_1 Transient receptor potential cation channel subfamily V member 3 (chains A, B, C, D) MEKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKT SPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRL KKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNI NPNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGA DVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNI LHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKY ILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEM LTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKM GWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFL YLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLL GFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLI TYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGE LCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAF EEVEEFPETSVVDAGLEVLFQGPAAAVDYKDDDDKAHHHHHHHHHH
Conformational ensemble of the human TRPV3 ion channel. Zubcevic, L., Herzik Jr., M.A., Wu, M. et al. Nat Commun (2018) 9:4773-4773. DOI 10.1038/s41467-018-07117-w · 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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