Structure of human TRPV3. Determined by electron microscopy at 3.54 Å resolution. Released 9 Nov 2022.
Explore 7XJ3 in 3D Show helices and sheets RCSB PDB PDBe
7XJ3 contains 126 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 | 120-129 | 10 | |
| α-helix | 133-147 | 15 | |
| α-helix | 155-162 | 8 | |
| α-helix | 171-176 | 6 | |
| α-helix | 183-196 | 14 | |
| α-helix | 200-204 | 5 | |
| α-helix | 218-224 | 7 | |
| α-helix | 229-237 | 9 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-306 | 8 | |
| α-helix | 317-326 | 10 | |
| α-helix | 344-350 | 7 | |
| α-helix | 355-361 | 7 | |
| 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 | 483-505 | 23 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-559 | 13 | |
| α-helix | 562-567 | 6 | |
| α-helix | 570-582 | 13 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 7 |
| α-helix | 610-611 | 2 | |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 7 |
| α-helix | 651-662 | 12 | |
| α-helix | 663-669 | 7 | |
| α-helix | 670-703 | 34 | |
| α-helix | 709-715 | 7 | |
| β-strand | 719-721 | 3 | 6 |
| β-strand | 729-737 | 9 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 120-129 | 10 | |
| α-helix | 133-147 | 15 | |
| α-helix | 155-162 | 8 | |
| β-strand | 163 | 1 | 1 |
| β-strand | 170 | 1 | 1 |
| α-helix | 171-176 | 6 | |
| α-helix | 183-196 | 14 | |
| α-helix | 200-204 | 5 | |
| α-helix | 218-224 | 7 | |
| α-helix | 229-236 | 8 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-306 | 8 | |
| α-helix | 317-326 | 10 | |
| α-helix | 344-350 | 7 | |
| α-helix | 354-361 | 8 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-378 | 3 | 2 |
| β-strand | 385-391 | 7 | 2 |
| α-helix | 403-409 | 7 | |
| α-helix | 423-432 | 10 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-460 | 23 | |
| α-helix | 483-505 | 23 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-559 | 13 | |
| α-helix | 562-567 | 6 | |
| α-helix | 570-582 | 13 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 3 |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 3 |
| α-helix | 651-662 | 12 | |
| α-helix | 663-669 | 7 | |
| α-helix | 670-703 | 34 | |
| α-helix | 709-715 | 7 | |
| β-strand | 719-721 | 3 | 2 |
| β-strand | 729-737 | 9 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 120-129 | 10 | |
| α-helix | 133-147 | 15 | |
| α-helix | 155-162 | 8 | |
| α-helix | 171-176 | 6 | |
| α-helix | 183-196 | 14 | |
| α-helix | 200-204 | 5 | |
| α-helix | 218-224 | 7 | |
| α-helix | 229-237 | 9 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-306 | 8 | |
| α-helix | 317-326 | 10 | |
| α-helix | 344-350 | 7 | |
| α-helix | 354-361 | 8 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-378 | 3 | 4 |
| β-strand | 385-391 | 7 | 4 |
| α-helix | 403-409 | 7 | |
| α-helix | 423-432 | 10 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-460 | 23 | |
| α-helix | 483-505 | 23 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-559 | 13 | |
| α-helix | 562-567 | 6 | |
| α-helix | 570-582 | 13 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 5 |
| α-helix | 617-619 | 3 | |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 5 |
| α-helix | 651-662 | 12 | |
| α-helix | 663-669 | 7 | |
| α-helix | 670-703 | 34 | |
| α-helix | 709-715 | 7 | |
| β-strand | 719-721 | 3 | 4 |
| β-strand | 729-737 | 9 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 120-129 | 10 | |
| α-helix | 133-147 | 15 | |
| α-helix | 155-162 | 8 | |
| β-strand | 163 | 1 | 8 |
| β-strand | 170 | 1 | 8 |
| α-helix | 171-176 | 6 | |
| α-helix | 183-196 | 14 | |
| α-helix | 200-204 | 5 | |
| α-helix | 218-224 | 7 | |
| α-helix | 229-236 | 8 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-306 | 8 | |
| α-helix | 317-326 | 10 | |
| α-helix | 344-350 | 7 | |
| α-helix | 355-361 | 7 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-378 | 3 | 9 |
| β-strand | 385-391 | 7 | 9 |
| α-helix | 403-409 | 7 | |
| α-helix | 423-432 | 10 | |
| α-helix | 433-437 | 5 | |
| α-helix | 438-460 | 23 | |
| α-helix | 483-505 | 23 | |
| α-helix | 522-541 | 20 | |
| α-helix | 547-559 | 13 | |
| α-helix | 562-567 | 6 | |
| α-helix | 570-582 | 13 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-608 | 21 | |
| β-strand | 609 | 1 | 10 |
| α-helix | 625-637 | 13 | |
| β-strand | 648 | 1 | 10 |
| α-helix | 651-662 | 12 | |
| α-helix | 663-669 | 7 | |
| α-helix | 670-703 | 34 | |
| α-helix | 709-715 | 7 | |
| β-strand | 719-721 | 3 | 9 |
| β-strand | 729-737 | 9 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| fusion of transient receptor potential cation channel subfamily V member 3 and 3C-GFP | A, B, C, D | protein | 1061 | Homo sapiens | Q8NET8 (AlphaFold model) |
>7XJ3_1 fusion of transient receptor potential cation channel subfamily V member 3 and 3C-GFP (chains A, B, C, D) MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTS PPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLK KRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNIN PNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGAD VNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNIL HALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYI LSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEML TLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMG WLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLY LFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLG FGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLIT YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGEL CKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTADFNKIQDSSRNNSKTTLNAF EEVEEFPETSVLEVLFQGPSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKL TLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKD DGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIK ANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLE FVTAAGITHGMDEWSHPQFEKGGGSGGGSGGSAWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6OU | [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y… | C39 H76 N O8 P | 14 |
Structural basis of TRPV3 inhibition by an antagonist. Fan, J., Hu, L., Yue, Z. et al. Nat Chem Biol (2023) 19:81-90. DOI 10.1038/s41589-022-01166-5 · 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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