Wildtype rabbit TRPV5 in nanodics in the presence of Menthol and PI(4,5)P2. Determined by electron microscopy at 3.37 Å resolution. Released 22 Apr 2026.
Explore 9O6G in 3D Show helices and sheets RCSB PDB PDBe
9O6G contains 148 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 | 30-46 | 17 | |
| α-helix | 48-55 | 8 | |
| α-helix | 58-66 | 9 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-98 | 7 | |
| α-helix | 103-105 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-126 | 7 | |
| α-helix | 130-138 | 9 | |
| α-helix | 166-173 | 8 | |
| α-helix | 176-184 | 9 | |
| α-helix | 199-204 | 6 | |
| α-helix | 210-221 | 12 | |
| α-helix | 232-234 | 3 | |
| α-helix | 243-249 | 7 | |
| α-helix | 253-260 | 8 | |
| β-strand | 265-270 | 6 | 1 |
| β-strand | 273-279 | 7 | 1 |
| α-helix | 292-297 | 6 | |
| α-helix | 302-306 | 5 | |
| 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 | 380-410 | 31 | |
| α-helix | 412-416 | 5 | |
| α-helix | 423-444 | 22 | |
| α-helix | 453-463 | 11 | |
| α-helix | 465-469 | 5 | |
| α-helix | 476-484 | 9 | |
| α-helix | 485-489 | 5 | |
| α-helix | 490-511 | 22 | |
| β-strand | 515 | 1 | 4 |
| α-helix | 526-537 | 12 | |
| α-helix | 542-544 | 3 | |
| α-helix | 553-562 | 10 | |
| α-helix | 563-570 | 8 | |
| α-helix | 571-586 | 16 | |
| α-helix | 589-607 | 19 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618 | 1 | 1 |
| β-strand | 630-636 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-46 | 17 | |
| α-helix | 48-55 | 8 | |
| α-helix | 58-66 | 9 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-100 | 9 | |
| α-helix | 103-107 | 5 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-126 | 7 | |
| α-helix | 131-139 | 9 | |
| α-helix | 166-173 | 8 | |
| α-helix | 177-184 | 8 | |
| α-helix | 199-205 | 7 | |
| α-helix | 209-221 | 13 | |
| α-helix | 243-249 | 7 | |
| α-helix | 253-260 | 8 | |
| β-strand | 266-270 | 5 | 5 |
| β-strand | 273-279 | 7 | 5 |
| α-helix | 292-298 | 7 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 6 |
| β-strand | 366 | 1 | 4 |
| β-strand | 368-370 | 3 | 6 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-410 | 31 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-463 | 13 | |
| α-helix | 464-471 | 8 | |
| α-helix | 477-484 | 8 | |
| α-helix | 485-489 | 5 | |
| α-helix | 490-511 | 22 | |
| β-strand | 515 | 1 | 7 |
| α-helix | 526-537 | 12 | |
| α-helix | 542-544 | 3 | |
| α-helix | 553-564 | 12 | |
| α-helix | 565-570 | 6 | |
| α-helix | 571-586 | 16 | |
| α-helix | 589-607 | 19 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-619 | 2 | 5 |
| β-strand | 629-635 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-46 | 17 | |
| α-helix | 48-55 | 8 | |
| α-helix | 58-65 | 8 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 105-107 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 120-127 | 8 | |
| α-helix | 130-139 | 10 | |
| α-helix | 166-173 | 8 | |
| α-helix | 177-184 | 8 | |
| α-helix | 199-205 | 7 | |
| α-helix | 213-221 | 9 | |
| α-helix | 243-249 | 7 | |
| α-helix | 253-260 | 8 | |
| β-strand | 265-270 | 6 | 8 |
| β-strand | 273-279 | 7 | 8 |
| α-helix | 292-297 | 6 | |
| α-helix | 302-307 | 6 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 9 |
| β-strand | 366 | 1 | 7 |
| β-strand | 368-370 | 3 | 9 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-410 | 31 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-463 | 13 | |
| α-helix | 464-471 | 8 | |
| α-helix | 476-484 | 9 | |
| α-helix | 485-490 | 6 | |
| α-helix | 491-492 | 2 | |
| α-helix | 494-511 | 18 | |
| β-strand | 515 | 1 | 10 |
| α-helix | 526-537 | 12 | |
| α-helix | 542-544 | 3 | |
| α-helix | 553-562 | 10 | |
| α-helix | 563-570 | 8 | |
| α-helix | 571-586 | 16 | |
| α-helix | 589-607 | 19 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618 | 1 | 8 |
| β-strand | 630-636 | 7 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-46 | 17 | |
| α-helix | 48-55 | 8 | |
| α-helix | 58-68 | 11 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-107 | 5 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-126 | 7 | |
| α-helix | 130-139 | 10 | |
| α-helix | 166-173 | 8 | |
| α-helix | 176-185 | 10 | |
| α-helix | 199-204 | 6 | |
| α-helix | 209-221 | 13 | |
| α-helix | 232-234 | 3 | |
| α-helix | 243-250 | 8 | |
| α-helix | 253-260 | 8 | |
| β-strand | 265-270 | 6 | 11 |
| β-strand | 273-279 | 7 | 11 |
| α-helix | 292-297 | 6 | |
| α-helix | 304-307 | 4 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 12 |
| β-strand | 366 | 1 | 10 |
| β-strand | 368-370 | 3 | 12 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-410 | 31 | |
| α-helix | 412-416 | 5 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-461 | 11 | |
| α-helix | 465-471 | 7 | |
| α-helix | 476-484 | 9 | |
| α-helix | 485-490 | 6 | |
| α-helix | 491-511 | 21 | |
| β-strand | 515 | 1 | 3 |
| α-helix | 526-537 | 12 | |
| α-helix | 542-544 | 3 | |
| α-helix | 553-562 | 10 | |
| α-helix | 563-570 | 8 | |
| α-helix | 571-587 | 17 | |
| α-helix | 589-607 | 19 | |
| α-helix | 610-612 | 3 | |
| α-helix | 614-615 | 2 | |
| β-strand | 618 | 1 | 11 |
| β-strand | 630-636 | 7 | 11 |
| 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) |
>9O6G_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 |
|---|---|---|---|
| ERG | Ergosterol | C28 H44 O | 8 |
| CPL | 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine | C42 H80 N O8 P | 16 |
| 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 |
| IT9 | (-)-Isopiperitenone | C10 H14 O | 1 |
Molecular mechanism of action of menthol, a novel inhibitor of TRPV5 channels. Mendez-Resendiz, A., De Jesus-Perez, J.J., Rangel-Yescas, G.E. et al. To be published.
Other PDB entries of the same protein (UniProt Q9XSM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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