Cryo-EM structure of TRPV5 in nanodiscs at pH6 state 3. Determined by electron microscopy at 2.6 Å resolution. Released 4 May 2022.
Explore 7T6O in 3D Show helices and sheets RCSB PDB PDBe
7T6O 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 | 30-46 | 17 | |
| α-helix | 48-54 | 7 | |
| α-helix | 58-65 | 8 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-106 | 4 | |
| 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 | 209-220 | 12 | |
| α-helix | 232-234 | 3 | |
| α-helix | 243-249 | 7 | |
| 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 | 303-309 | 7 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 2 |
| α-helix | 358-359 | 2 | |
| β-strand | 366 | 1 | 3 |
| β-strand | 368-370 | 3 | 2 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-409 | 30 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-463 | 13 | |
| α-helix | 464-471 | 8 | |
| α-helix | 475-486 | 12 | |
| α-helix | 489-511 | 23 | |
| β-strand | 515 | 1 | 4 |
| α-helix | 526-537 | 12 | |
| α-helix | 550-552 | 3 | |
| α-helix | 553-562 | 10 | |
| α-helix | 563-570 | 8 | |
| α-helix | 571-584 | 14 | |
| α-helix | 586-607 | 22 | |
| α-helix | 610-612 | 3 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-619 | 2 | 1 |
| α-helix | 621-623 | 3 | |
| β-strand | 629-636 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-46 | 17 | |
| α-helix | 48-54 | 7 | |
| α-helix | 58-65 | 8 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-106 | 4 | |
| 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 | 209-220 | 12 | |
| α-helix | 232-234 | 3 | |
| α-helix | 243-249 | 7 | |
| α-helix | 253-261 | 9 | |
| β-strand | 264-270 | 7 | 5 |
| β-strand | 273-279 | 7 | 5 |
| α-helix | 281-284 | 4 | |
| α-helix | 292-297 | 6 | |
| α-helix | 303-309 | 7 | |
| α-helix | 311-320 | 10 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 6 |
| α-helix | 358-359 | 2 | |
| β-strand | 366 | 1 | 4 |
| β-strand | 368-370 | 3 | 6 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-409 | 30 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-463 | 13 | |
| α-helix | 464-471 | 8 | |
| α-helix | 475-486 | 12 | |
| α-helix | 489-511 | 23 | |
| β-strand | 515 | 1 | 7 |
| α-helix | 526-537 | 12 | |
| α-helix | 550-552 | 3 | |
| α-helix | 553-562 | 10 | |
| α-helix | 563-571 | 9 | |
| α-helix | 572-584 | 13 | |
| α-helix | 586-607 | 22 | |
| α-helix | 610-612 | 3 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-619 | 2 | 5 |
| α-helix | 621-623 | 3 | |
| β-strand | 629-636 | 8 | 5 |
| 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) |
>7T6O_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
Structural basis of TRPV5 regulation by physiological and pathophysiological modulators. Fluck, E.C., Yazici, A.T., Rohacs, T. et al. Cell Rep (2022) 39:110737-110737. DOI 10.1016/j.celrep.2022.110737 · 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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