Wildtype rabbit TRPV5 into nanodiscs in the presence of PI(4,5)P2 and ruthenium red. Determined by electron microscopy at 2.65 Å resolution. Released 7 Feb 2024.
Explore 8FFQ in 3D Show helices and sheets RCSB PDB PDBe
8FFQ contains 164 α-helices and 32 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 | 29-46 | 18 | |
| α-helix | 48-55 | 8 | |
| α-helix | 58-64 | 7 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 120-126 | 7 | |
| α-helix | 130-138 | 9 | |
| α-helix | 150-152 | 3 | |
| α-helix | 166-172 | 7 | |
| α-helix | 176-184 | 9 | |
| α-helix | 199-204 | 6 | |
| α-helix | 211-220 | 10 | |
| α-helix | 232-234 | 3 | |
| α-helix | 243-250 | 8 | |
| α-helix | 253-261 | 9 | |
| β-strand | 264-270 | 7 | 1 |
| β-strand | 273-279 | 7 | 1 |
| α-helix | 281-284 | 4 | |
| α-helix | 292-297 | 6 | |
| α-helix | 302-309 | 8 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 2 |
| β-strand | 366 | 1 | 3 |
| β-strand | 368-370 | 3 | 2 |
| α-helix | 371-372 | 2 | |
| α-helix | 373-376 | 4 | |
| α-helix | 380-410 | 31 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-464 | 14 | |
| α-helix | 465-471 | 7 | |
| α-helix | 476-485 | 10 | |
| α-helix | 486-490 | 5 | |
| α-helix | 491-512 | 22 | |
| β-strand | 515 | 1 | 4 |
| α-helix | 526-537 | 12 | |
| α-helix | 542-544 | 3 | |
| α-helix | 553-562 | 10 | |
| α-helix | 563-571 | 9 | |
| α-helix | 572-607 | 36 | |
| α-helix | 610-612 | 3 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-619 | 2 | 1 |
| α-helix | 620-623 | 4 | |
| β-strand | 629-636 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily V member 5 | A, B, C, D | protein | 739 | Oryctolagus cuniculus | Q9XSM3 (AlphaFold model) |
>8FFQ_1 Transient receptor potential cation channel subfamily V member 5 (chains A, B, C, D) MGACPPKAKGPWAQLQKLLISWPVGEQDWEQYRDRVNMLQQERIRDSPLLQAAKENDLRL LKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKEPALCEPFVGQTA LHIAVMNQNLNLVRALLARGASVSARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVR LLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQG LTPFKLAGVEGNTVMFQHLMQKRKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSSK KREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLKLRDDNRT DPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTI LGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTI MIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGEFSDYPTALFSTFELFLTI IDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVAT TVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHHDQNPLRVLRYVEAFKCSDKEDGQ EQLSEKRPSTVESGMLSRASVAFQTPSLSRTTSQSSNSHRGWEILRRNTLGHLNLGLDLG EGDGEEVYHFTETSQVAPA
| ID | Name | Formula | Copies |
|---|---|---|---|
| CPL | 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine | C42 H80 N O8 P | 4 |
| R2R | ruthenium(6+) azanide pentaamino(oxido)ruthenium (1/4/2) | H42 N14 O2 Ru3 | 1 |
| ERG | Ergosterol | C28 H44 O | 8 |
Molecular details of ruthenium red pore block in TRPV channels. Pumroy, R.A., De Jesus-Perez, J.J., Protopopova, A.D. et al. EMBO Rep (2024) 25:506-523. DOI 10.1038/s44319-023-00050-0 · PubMed
Other PDB entries of the same protein (UniProt Q9XSM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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