Cryo-EM structure of human TRPV3 determined in lipid nanodisc. Determined by electron microscopy at 3.1 Å resolution. Released 1 Jul 2020.
Explore 6UW4 in 3D Show helices and sheets RCSB PDB PDBe
6UW4 contains 128 α-helices and 28 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 | 132-145 | 14 | |
| α-helix | 155-162 | 8 | |
| β-strand | 163 | 1 | 1 |
| β-strand | 170 | 1 | 1 |
| α-helix | 171-176 | 6 | |
| α-helix | 183-195 | 13 | |
| α-helix | 200-203 | 4 | |
| α-helix | 218-224 | 7 | |
| α-helix | 228-235 | 8 | |
| α-helix | 265-270 | 6 | |
| α-helix | 275-283 | 9 | |
| α-helix | 299-306 | 8 | |
| α-helix | 316-328 | 13 | |
| α-helix | 344-351 | 8 | |
| α-helix | 354-361 | 8 | |
| β-strand | 376-382 | 7 | 2 |
| β-strand | 385-390 | 6 | 2 |
| α-helix | 403-408 | 6 | |
| α-helix | 416-418 | 3 | |
| α-helix | 423-432 | 10 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-461 | 24 | |
| α-helix | 482-484 | 3 | |
| α-helix | 485-505 | 21 | |
| α-helix | 521-540 | 20 | |
| α-helix | 547-560 | 14 | |
| α-helix | 561-566 | 6 | |
| α-helix | 570-582 | 13 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-607 | 20 | |
| β-strand | 609 | 1 | 3 |
| α-helix | 625-636 | 12 | |
| β-strand | 648 | 1 | 3 |
| α-helix | 651-662 | 12 | |
| α-helix | 663-669 | 7 | |
| α-helix | 670-684 | 15 | |
| α-helix | 688-706 | 19 | |
| β-strand | 733-737 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 3 | A, B, C, D | protein | 790 | Homo sapiens | Q8NET8 (AlphaFold model) |
>6UW4_1 Transient receptor potential cation channel subfamily V member 3 (chains A, B, C, D) MKAHPKEMVPLMGKRVAAPSGNPAVLPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTS PPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLK KRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNIN PNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGAD VNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNIL HALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYI LSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEML TLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMG WLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLY LFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLG FGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLIT YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGEL CKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAFE EVEEFPETSV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6OU | [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y… | C39 H76 N O8 P | 20 |
Water and common crystallization additives (NA) are not listed.
Gating of human TRPV3 in a lipid bilayer. Deng, Z., Maksaev, G., Rau, M. et al. Nat Struct Mol Biol (2020) 27:635-644. DOI 10.1038/s41594-020-0428-2 · 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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