Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc. Determined by electron microscopy at 2.95 Å resolution. Released 25 May 2016.
Explore 5IRX in 3D Show helices and sheets RCSB PDB PDBe
5IRX contains 94 α-helices and 60 β-strands across 6 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 | 336-341 | 6 | |
| α-helix | 346-353 | 8 | |
| β-strand | 369-374 | 6 | 1 |
| β-strand | 377-381 | 5 | 1 |
| α-helix | 395-400 | 6 | |
| α-helix | 412-415 | 4 | |
| α-helix | 419-425 | 7 | |
| α-helix | 426-430 | 5 | |
| α-helix | 431-453 | 23 | |
| α-helix | 462-463 | 2 | |
| α-helix | 469-498 | 30 | |
| α-helix | 511-531 | 21 | |
| α-helix | 537-550 | 14 | |
| α-helix | 551-554 | 4 | |
| β-strand | 557 | 1 | 2 |
| β-strand | 559 | 1 | 2 |
| α-helix | 564-571 | 8 | |
| α-helix | 572-577 | 6 | |
| α-helix | 578-580 | 3 | |
| α-helix | 584-598 | 15 | |
| α-helix | 630-641 | 12 | |
| α-helix | 656-667 | 12 | |
| α-helix | 668-674 | 7 | |
| α-helix | 675-691 | 17 | |
| α-helix | 693-712 | 20 | |
| α-helix | 716-719 | 4 | |
| β-strand | 724-725 | 2 | 3 |
| β-strand | 739-740 | 2 | 3 |
| β-strand | 743-746 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 13 |
| β-strand | 5 | 1 | 14 |
| β-strand | 7 | 1 | 14 |
| β-strand | 8 | 1 | 15 |
| β-strand | 15 | 1 | 13 |
| β-strand | 22 | 1 | 16 |
| β-strand | 30 | 1 | 15 |
| β-strand | 32 | 1 | 16 |
| α-helix | 33-36 | 4 | |
| β-strand | 45 | 1 | 17 |
| β-strand | 50 | 1 | 18 |
| β-strand | 51 | 1 | 19 |
| β-strand | 55 | 1 | 19 |
| β-strand | 57 | 1 | 17 |
| β-strand | 62 | 1 | 20 |
| α-helix | 69 | 1 | |
| β-strand | 70 | 1 | 18 |
| α-helix | 71 | 1 | |
| β-strand | 72 | 1 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 1 | A, B, C, D | protein | 636 | Rattus norvegicus | O35433 (AlphaFold model) |
| Tau-theraphotoxin-Hs1a | E, F | protein | 75 | Haplopelma schmidti | P0CH43 (AlphaFold model) |
>5IRX_1 Transient receptor potential cation channel subfamily V member 1 (chains A, B, C, D) AMGSRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNL HNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGA DVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGN TVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGK IGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSE TPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKL KNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLV SVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYL VFLFGFSTAVVTLIEDGKYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVI LTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQV GFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPG
>5IRX_2 Tau-theraphotoxin-Hs1a (chains E, F) DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPVTTNCAKEGEVCGWGSKCCHG LDCPLAFIPYCEKYR
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6O9 | (2S)-2-(acetyloxy)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}propyl… | C12 H24 N O8 P | 4 |
| 6EU | resiniferatoxin | C37 H40 O9 | 4 |
| 6OE | (2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl… | C17 H34 N O8 P | 8 |
| 6O8 | (4R,7S)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(pentanoyloxy)methyl]-3,5,8-trio… | C19 H39 N O8 P | 4 |
TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Gao, Y., Cao, E., Julius, D. et al. Nature (2016) 534:347-351. DOI 10.1038/nature17964 · 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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