Cryo-EM structure of TRPV5 at pH8 in nanodiscs. Determined by electron microscopy at 3.2 Å resolution. Released 4 May 2022.
Explore 7T6J in 3D Show helices and sheets RCSB PDB PDBe
7T6J contains 144 α-helices and 24 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 | 92-101 | 10 | |
| α-helix | 103-105 | 3 | |
| α-helix | 120-126 | 7 | |
| α-helix | 130-138 | 9 | |
| α-helix | 166-173 | 8 | |
| α-helix | 176-184 | 9 | |
| α-helix | 194-196 | 3 | |
| α-helix | 199-204 | 6 | |
| α-helix | 211-221 | 11 | |
| α-helix | 243-250 | 8 | |
| α-helix | 254-261 | 8 | |
| β-strand | 264-268 | 5 | 1 |
| β-strand | 273-279 | 7 | 1 |
| α-helix | 281-284 | 4 | |
| α-helix | 292-297 | 6 | |
| α-helix | 303-307 | 5 | |
| α-helix | 313-319 | 7 | |
| α-helix | 320-325 | 6 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 2 |
| β-strand | 368-370 | 3 | 2 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-401 | 22 | |
| α-helix | 405-408 | 4 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-463 | 13 | |
| α-helix | 464-471 | 8 | |
| α-helix | 476-486 | 11 | |
| α-helix | 489-511 | 23 | |
| α-helix | 526-535 | 10 | |
| α-helix | 542-543 | 2 | |
| α-helix | 553-565 | 13 | |
| α-helix | 570-604 | 35 | |
| α-helix | 610-612 | 3 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-619 | 2 | 1 |
| β-strand | 629-636 | 8 | 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 | 92-101 | 10 | |
| α-helix | 103-105 | 3 | |
| α-helix | 120-126 | 7 | |
| α-helix | 130-138 | 9 | |
| α-helix | 166-173 | 8 | |
| α-helix | 176-184 | 9 | |
| α-helix | 194-196 | 3 | |
| α-helix | 199-204 | 6 | |
| α-helix | 211-221 | 11 | |
| α-helix | 243-250 | 8 | |
| α-helix | 254-261 | 8 | |
| β-strand | 264-268 | 5 | 7 |
| β-strand | 273-279 | 7 | 7 |
| α-helix | 281-284 | 4 | |
| α-helix | 292-297 | 6 | |
| α-helix | 303-309 | 7 | |
| α-helix | 313-319 | 7 | |
| α-helix | 320-325 | 6 | |
| α-helix | 326-348 | 23 | |
| β-strand | 352-354 | 3 | 8 |
| β-strand | 368-370 | 3 | 8 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-401 | 22 | |
| α-helix | 405-408 | 4 | |
| α-helix | 412-417 | 6 | |
| α-helix | 423-444 | 22 | |
| α-helix | 451-463 | 13 | |
| α-helix | 464-471 | 8 | |
| α-helix | 476-486 | 11 | |
| α-helix | 489-511 | 23 | |
| α-helix | 526-535 | 10 | |
| α-helix | 542-543 | 2 | |
| α-helix | 553-565 | 13 | |
| α-helix | 570-604 | 35 | |
| α-helix | 610-612 | 3 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-619 | 2 | 7 |
| β-strand | 629-636 | 8 | 7 |
| 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) |
>7T6J_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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