Cryo-EM structure of unliganded full-length TRPV1 at neutral pH. Determined by electron microscopy at 2.63 Å resolution. Released 22 Sept 2021.
Explore 7L2H in 3D Show helices and sheets RCSB PDB PDBe
7L2H contains 116 α-helices and 26 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 | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-269 | 9 | |
| α-helix | 287-293 | 7 | |
| α-helix | 299-319 | 21 | |
| α-helix | 336-342 | 7 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 1 |
| β-strand | 377-383 | 7 | 1 |
| α-helix | 395-400 | 6 | |
| α-helix | 412-414 | 3 | |
| α-helix | 416-425 | 10 | |
| α-helix | 426-430 | 5 | |
| α-helix | 431-453 | 23 | |
| α-helix | 463-466 | 4 | |
| α-helix | 469-499 | 31 | |
| α-helix | 505-508 | 4 | |
| α-helix | 511-531 | 21 | |
| α-helix | 537-550 | 14 | |
| α-helix | 551-556 | 6 | |
| α-helix | 560-572 | 13 | |
| α-helix | 573-577 | 5 | |
| α-helix | 578-598 | 21 | |
| α-helix | 630-641 | 12 | |
| α-helix | 656-666 | 11 | |
| α-helix | 667-675 | 9 | |
| α-helix | 676-687 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726-730 | 5 | 2 |
| β-strand | 736-738 | 3 | 2 |
| β-strand | 741-747 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-268 | 8 | |
| α-helix | 274-276 | 3 | |
| α-helix | 287-293 | 7 | |
| α-helix | 299-319 | 21 | |
| α-helix | 325-327 | 3 | |
| α-helix | 336-342 | 7 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 6 |
| β-strand | 377-383 | 7 | 6 |
| α-helix | 395-400 | 6 | |
| α-helix | 412-414 | 3 | |
| α-helix | 416-425 | 10 | |
| α-helix | 426-430 | 5 | |
| α-helix | 431-453 | 23 | |
| α-helix | 463-466 | 4 | |
| α-helix | 469-499 | 31 | |
| α-helix | 505-508 | 4 | |
| α-helix | 511-531 | 21 | |
| α-helix | 537-551 | 15 | |
| α-helix | 552-556 | 5 | |
| α-helix | 560-572 | 13 | |
| α-helix | 573-577 | 5 | |
| α-helix | 578-598 | 21 | |
| β-strand | 599 | 1 | 7 |
| α-helix | 630-641 | 12 | |
| β-strand | 653 | 1 | 7 |
| α-helix | 656-666 | 11 | |
| α-helix | 667-675 | 9 | |
| α-helix | 676-687 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726-730 | 5 | 8 |
| β-strand | 736-738 | 3 | 8 |
| β-strand | 741-747 | 7 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-268 | 8 | |
| α-helix | 287-293 | 7 | |
| α-helix | 299-319 | 21 | |
| α-helix | 336-342 | 7 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 9 |
| β-strand | 377-383 | 7 | 9 |
| α-helix | 395-400 | 6 | |
| α-helix | 412-414 | 3 | |
| α-helix | 416-425 | 10 | |
| α-helix | 426-430 | 5 | |
| α-helix | 431-453 | 23 | |
| α-helix | 463-466 | 4 | |
| α-helix | 469-499 | 31 | |
| α-helix | 505-508 | 4 | |
| α-helix | 511-531 | 21 | |
| α-helix | 537-550 | 14 | |
| α-helix | 551-556 | 6 | |
| α-helix | 560-572 | 13 | |
| α-helix | 573-577 | 5 | |
| α-helix | 578-598 | 21 | |
| β-strand | 599 | 1 | 10 |
| α-helix | 630-641 | 12 | |
| β-strand | 653 | 1 | 10 |
| α-helix | 656-666 | 11 | |
| α-helix | 667-675 | 9 | |
| α-helix | 676-687 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726-730 | 5 | 11 |
| β-strand | 736-738 | 3 | 11 |
| β-strand | 741-747 | 7 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 229-231 | 3 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-269 | 9 | |
| α-helix | 274-276 | 3 | |
| α-helix | 287-293 | 7 | |
| α-helix | 299-319 | 21 | |
| α-helix | 336-342 | 7 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 3 |
| β-strand | 377-383 | 7 | 3 |
| α-helix | 395-400 | 6 | |
| α-helix | 412-414 | 3 | |
| α-helix | 416-425 | 10 | |
| α-helix | 426-430 | 5 | |
| α-helix | 431-453 | 23 | |
| α-helix | 463-466 | 4 | |
| α-helix | 469-499 | 31 | |
| α-helix | 505-508 | 4 | |
| α-helix | 511-531 | 21 | |
| α-helix | 537-551 | 15 | |
| α-helix | 552-556 | 5 | |
| α-helix | 560-572 | 13 | |
| α-helix | 573-577 | 5 | |
| α-helix | 578-598 | 21 | |
| β-strand | 599 | 1 | 4 |
| α-helix | 630-641 | 12 | |
| β-strand | 653 | 1 | 4 |
| α-helix | 656-667 | 12 | |
| α-helix | 668-675 | 8 | |
| α-helix | 676-688 | 13 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726-730 | 5 | 5 |
| β-strand | 736-738 | 3 | 5 |
| β-strand | 741-747 | 7 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 1 | A, B, C, D | protein | 842 | Rattus norvegicus | O35433 (AlphaFold model) |
>7L2H_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D) GAMGSEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSE EASPLDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRS IFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALL LDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFF KKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVAD NTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQRE IHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVE PLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVT GEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKE YVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVV TLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFK AVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCM RKAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFS LRSGRVSGRNWKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPG EK
| ID | Name | Formula | Copies |
|---|---|---|---|
| XJ7 | (2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2R,3S,4S,5R,6S)-2,3,4,5,6-pentahydrox… | C26 H49 O13 P | 4 |
| XJD | (10R,13S)-16-amino-13-hydroxy-7,13-dioxo-8,12,14-trioxa-13lambda~5~-phosphahexa… | C25 H50 N O8 P | 4 |
Water and common crystallization additives (NA) are not listed.
Structural snapshots of TRPV1 reveal mechanism of polymodal functionality. Zhang, K., Julius, D., Cheng, Y. Cell (2021) 184:5138. DOI 10.1016/j.cell.2021.08.012 · PubMed
Other PDB entries of the same protein (UniProt O35433 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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