cryo-EM structure of DkTx-bound minimal TRPV1 at the pre-bound state. Determined by electron microscopy at 2.71 Å resolution. Released 22 Sept 2021.
Explore 7L2S in 3D Show helices and sheets RCSB PDB PDBe
7L2S contains 150 α-helices and 38 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 | 115-123 | 9 | |
| α-helix | 126-129 | 4 | |
| α-helix | 132-139 | 8 | |
| α-helix | 146-148 | 3 | |
| α-helix | 157-163 | 7 | |
| β-strand | 166 | 1 | 6 |
| β-strand | 169 | 1 | 6 |
| α-helix | 172-183 | 12 | |
| α-helix | 187-190 | 4 | |
| β-strand | 193 | 1 | 7 |
| β-strand | 203 | 1 | 7 |
| α-helix | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 234-236 | 3 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-269 | 9 | |
| α-helix | 287-293 | 7 | |
| α-helix | 299-319 | 21 | |
| α-helix | 325-327 | 3 | |
| α-helix | 336-343 | 8 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 8 |
| β-strand | 377-382 | 6 | 8 |
| 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 | 503-508 | 6 | |
| 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 | 630-638 | 9 | |
| α-helix | 639-642 | 4 | |
| α-helix | 656-667 | 12 | |
| α-helix | 668-674 | 7 | |
| α-helix | 675-686 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726 | 1 | 9 |
| β-strand | 738 | 1 | 9 |
| β-strand | 742-747 | 6 | 8 |
| α-helix | 753-755 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-123 | 9 | |
| α-helix | 127-131 | 5 | |
| α-helix | 132-139 | 8 | |
| α-helix | 146-148 | 3 | |
| α-helix | 157-163 | 7 | |
| β-strand | 166 | 1 | 10 |
| β-strand | 169 | 1 | 10 |
| α-helix | 172-183 | 12 | |
| α-helix | 187-190 | 4 | |
| β-strand | 193 | 1 | 11 |
| β-strand | 203 | 1 | 11 |
| 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 | 325-327 | 3 | |
| α-helix | 336-343 | 8 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 12 |
| β-strand | 377-382 | 6 | 12 |
| 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 | 630-638 | 9 | |
| α-helix | 656-666 | 11 | |
| α-helix | 667-674 | 8 | |
| α-helix | 675-686 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726 | 1 | 13 |
| β-strand | 738 | 1 | 13 |
| β-strand | 742-747 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 114-123 | 10 | |
| α-helix | 126-131 | 6 | |
| α-helix | 135-139 | 5 | |
| α-helix | 146-148 | 3 | |
| α-helix | 157-162 | 6 | |
| β-strand | 166 | 1 | 14 |
| β-strand | 169 | 1 | 14 |
| α-helix | 172-183 | 12 | |
| α-helix | 187-190 | 4 | |
| β-strand | 193 | 1 | 15 |
| β-strand | 203 | 1 | 15 |
| α-helix | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 234-236 | 3 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-269 | 9 | |
| α-helix | 287-294 | 8 | |
| α-helix | 299-319 | 21 | |
| α-helix | 325-327 | 3 | |
| α-helix | 336-343 | 8 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 16 |
| β-strand | 377-382 | 6 | 16 |
| 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 | 462-465 | 4 | |
| α-helix | 469-499 | 31 | |
| α-helix | 505-508 | 4 | |
| α-helix | 511-530 | 20 | |
| 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 | 630-638 | 9 | |
| α-helix | 639-642 | 4 | |
| α-helix | 656-666 | 11 | |
| α-helix | 667-674 | 8 | |
| α-helix | 675-686 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726 | 1 | 17 |
| β-strand | 738 | 1 | 17 |
| β-strand | 742-747 | 6 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-123 | 9 | |
| α-helix | 127-129 | 3 | |
| α-helix | 132-139 | 8 | |
| α-helix | 146-148 | 3 | |
| β-strand | 149 | 1 | 1 |
| β-strand | 156 | 1 | 1 |
| α-helix | 157-163 | 7 | |
| β-strand | 166 | 1 | 2 |
| β-strand | 169 | 1 | 2 |
| α-helix | 172-183 | 12 | |
| α-helix | 187-190 | 4 | |
| β-strand | 193 | 1 | 3 |
| β-strand | 203 | 1 | 3 |
| α-helix | 204-210 | 7 | |
| α-helix | 214-222 | 9 | |
| α-helix | 234-236 | 3 | |
| α-helix | 251-257 | 7 | |
| α-helix | 261-269 | 9 | |
| α-helix | 287-293 | 7 | |
| α-helix | 299-319 | 21 | |
| α-helix | 325-327 | 3 | |
| α-helix | 336-343 | 8 | |
| α-helix | 346-353 | 8 | |
| α-helix | 363-365 | 3 | |
| β-strand | 368-373 | 6 | 4 |
| β-strand | 377-382 | 6 | 4 |
| 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 | 463-464 | 2 | |
| 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 | 630-638 | 9 | |
| α-helix | 656-667 | 12 | |
| α-helix | 668-674 | 7 | |
| α-helix | 675-686 | 12 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726 | 1 | 5 |
| β-strand | 738 | 1 | 5 |
| β-strand | 742-747 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 1 | A, B, C, D | protein | 637 | Rattus norvegicus | O35433 (AlphaFold model) |
>7L2S_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D) GAMGSRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLN LHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENG ADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVG NTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSG KIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSS ETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYK LKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFML VSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVY LVFLFGFSTAVVTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYV ILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQ VGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6IY | (10R,13S)-16-amino-13-hydroxy-7,13-dioxo-8,12,14-trioxa-13lambda~5~-phosphahexa… | C28 H56 N O8 P | 4 |
| XJ7 | (2S)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1r,2R,3S,4S,5R,6S)-2,3,4,5,6-pentahydrox… | C26 H49 O13 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) 184:5138-5150.e12. 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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