TRPV1 in nanodisc bound with diC8-PIP2 in the closed state. Determined by electron microscopy at 3.0 Å resolution. Released 8 May 2024.
Explore 8U30 in 3D Show helices and sheets RCSB PDB PDBe
8U30 contains 128 α-helices and 20 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 | 204-211 | 8 | |
| α-helix | 214-223 | 10 | |
| α-helix | 234-236 | 3 | |
| α-helix | 251-256 | 6 | |
| α-helix | 261-268 | 8 | |
| α-helix | 274-276 | 3 | |
| 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 | 368-374 | 7 | 1 |
| β-strand | 377-383 | 7 | 1 |
| α-helix | 395-400 | 6 | |
| α-helix | 411-414 | 4 | |
| α-helix | 416-425 | 10 | |
| α-helix | 426-430 | 5 | |
| α-helix | 431-453 | 23 | |
| α-helix | 469-499 | 31 | |
| α-helix | 505-507 | 3 | |
| 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 | |
| α-helix | 603-628 | 3 | |
| α-helix | 630-639 | 10 | |
| α-helix | 640-642 | 3 | |
| α-helix | 656-667 | 12 | |
| α-helix | 668-674 | 7 | |
| α-helix | 675-688 | 14 | |
| α-helix | 690-711 | 22 | |
| β-strand | 726 | 1 | 2 |
| β-strand | 738 | 1 | 2 |
| β-strand | 741-747 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 1 | A, B, C, D | protein | 815 | Rattus norvegicus | O35433 (AlphaFold model) |
>8U30_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D) MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASP LDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDA VAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVA RKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTK GRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVD NTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEP ECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNR LLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEIL SVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVAS MVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIE DGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMG ETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDYRWCFR VDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRD RHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| PIO | [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d… | C25 H49 O19 P3 | 4 |
Water and common crystallization additives (NA) are not listed.
Structural basis of TRPV1 modulation by endogenous bioactive lipids. Arnold, W.R., Mancino, A., Moss 3rd, F.R. et al. Nat Struct Mol Biol (2024) 31:1377-1385. DOI 10.1038/s41594-024-01299-2 · 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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