Cryo-EM structure of TRPV5 in nanodiscs with PI(4,5)P2 at pH6 state 1. Determined by electron microscopy at 2.8 Å resolution. Released 4 May 2022.
Explore 7T6M in 3D Show helices and sheets RCSB PDB PDBe
7T6M contains 152 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 | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-105 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-127 | 8 | |
| 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 | 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 | 304-307 | 4 | |
| 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 | 380-403 | 24 | |
| 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 | 476-483 | 8 | |
| α-helix | 484-490 | 7 | |
| α-helix | 491-510 | 20 | |
| 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 | 571-587 | 17 | |
| 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 | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-105 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-127 | 8 | |
| 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 | 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 | 304-307 | 4 | |
| 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 | 380-403 | 24 | |
| 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 | 476-483 | 8 | |
| α-helix | 484-490 | 7 | |
| α-helix | 491-510 | 20 | |
| β-strand | 515 | 1 | 7 |
| 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 | 614-616 | 3 | |
| β-strand | 618 | 1 | 5 |
| β-strand | 630-636 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-46 | 17 | |
| α-helix | 48-55 | 8 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-105 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-127 | 8 | |
| 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 | 243-249 | 7 | |
| α-helix | 253-261 | 9 | |
| β-strand | 264-270 | 7 | 8 |
| β-strand | 273-279 | 7 | 8 |
| α-helix | 281-284 | 4 | |
| 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 | 9 |
| β-strand | 366 | 1 | 10 |
| β-strand | 368-370 | 3 | 9 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-403 | 24 | |
| 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 | 476-483 | 8 | |
| α-helix | 484-490 | 7 | |
| α-helix | 491-510 | 20 | |
| 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 | 614-616 | 3 | |
| β-strand | 618 | 1 | 8 |
| α-helix | 621-623 | 3 | |
| β-strand | 630-636 | 7 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 30-46 | 17 | |
| α-helix | 48-55 | 8 | |
| α-helix | 82-88 | 7 | |
| α-helix | 92-101 | 10 | |
| α-helix | 103-105 | 3 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-127 | 8 | |
| 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 | 243-249 | 7 | |
| α-helix | 253-261 | 9 | |
| β-strand | 264-270 | 7 | 11 |
| β-strand | 273-279 | 7 | 11 |
| α-helix | 281-284 | 4 | |
| 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 | 7 |
| β-strand | 368-370 | 3 | 12 |
| α-helix | 371-372 | 2 | |
| α-helix | 380-403 | 24 | |
| 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 | 476-483 | 8 | |
| α-helix | 484-490 | 7 | |
| α-helix | 491-510 | 20 | |
| 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 | 571-587 | 17 | |
| α-helix | 589-607 | 19 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618 | 1 | 11 |
| α-helix | 621-623 | 3 | |
| 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) |
>7T6M_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 |
|---|---|---|---|
| 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 |
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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