7T6Q: TRPV5 T709D with PI(4,5)P2 in nanodiscs

Cryo-EM structure of TRPV5 T709D with PI(4,5)P2 in nanodiscs. Determined by electron microscopy at 3.4 Å resolution. Released 4 May 2022.

Method
Electron microscopy
Resolution
3.4 Å
Organism
Oryctolagus cuniculus
Chains
4
Atoms
19,600
Mol. weight
338.18 kDa
Ligands
PIO
Released
4 May 2022

Explore 7T6Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7T6Q contains 142 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.

Chain A: 36 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix31-4616
α-helix48-558
α-helix59-668
α-helix82-887
α-helix92-10110
α-helix103-1075
α-helix120-1267
α-helix130-1389
α-helix166-1738
α-helix176-1849
α-helix201-2044
α-helix211-22212
α-helix243-2508
α-helix253-26311
β-strand265-27061
β-strand273-27971
α-helix281-2844
α-helix292-2976
α-helix302-3054
α-helix314-3207
α-helix321-3255
α-helix326-34823
β-strand352-35432
β-strand368-37032
α-helix380-40021
α-helix404-4107
α-helix412-4154
α-helix423-44422
α-helix451-46313
α-helix464-4696
α-helix477-48812
α-helix493-4975
α-helix501-51010
α-helix526-53712
α-helix542-5432
α-helix553-56210
α-helix563-5708
α-helix571-58616
α-helix589-60517
α-helix614-6152
β-strand61811
β-strand630-63451
Chain B: 35 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix31-4616
α-helix48-558
α-helix59-668
α-helix82-887
α-helix92-10110
α-helix103-1075
α-helix120-1267
α-helix130-1389
α-helix166-1738
α-helix176-1849
α-helix199-2046
α-helix211-22111
α-helix243-2508
α-helix253-26311
β-strand265-27063
β-strand273-27973
α-helix281-2844
α-helix292-2976
α-helix302-3054
α-helix313-3208
α-helix321-3255
α-helix326-34823
β-strand352-35434
β-strand368-37034
α-helix380-40021
α-helix404-4107
α-helix412-4154
α-helix423-44422
α-helix451-46313
α-helix464-4696
α-helix478-49720
α-helix501-51111
α-helix526-53712
α-helix542-5432
α-helix553-56210
α-helix563-5708
α-helix571-58616
α-helix589-60517
α-helix614-6152
β-strand61813
β-strand630-63453
Chain C: 36 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix31-4616
α-helix48-558
α-helix59-668
α-helix82-887
α-helix92-10110
α-helix103-1075
α-helix120-1267
α-helix130-1389
α-helix166-1738
α-helix176-1849
α-helix201-2044
α-helix211-22212
α-helix243-2508
α-helix253-26311
β-strand265-27065
β-strand273-27975
α-helix281-2844
α-helix292-2976
α-helix302-3054
α-helix314-3207
α-helix321-3255
α-helix326-34823
β-strand352-35436
β-strand368-37036
α-helix380-40021
α-helix404-4107
α-helix412-4154
α-helix423-44422
α-helix451-46313
α-helix464-4696
α-helix476-4849
α-helix485-4895
α-helix501-51010
α-helix526-53712
α-helix542-5432
α-helix553-56210
α-helix563-5708
α-helix571-58616
α-helix589-60517
α-helix614-6163
β-strand61815
β-strand630-63455
Chain D: 35 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix31-4616
α-helix48-558
α-helix59-668
α-helix82-887
α-helix92-10110
α-helix103-1075
α-helix120-1267
α-helix130-1389
α-helix166-1738
α-helix176-1849
α-helix201-2044
α-helix211-22212
α-helix243-2508
α-helix253-26311
β-strand265-27067
β-strand273-27977
α-helix281-2844
α-helix292-2976
α-helix302-3054
α-helix314-3207
α-helix321-3255
α-helix326-34823
β-strand352-35438
β-strand368-37038
α-helix380-40021
α-helix404-4107
α-helix412-4154
α-helix423-44422
α-helix451-46313
α-helix464-4696
α-helix478-49215
α-helix501-51111
α-helix526-53712
α-helix542-5432
α-helix553-56210
α-helix563-5708
α-helix571-58616
α-helix589-60517
α-helix614-6152
β-strand61817
β-strand630-63457

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 5A, B, C, Dprotein739Oryctolagus cuniculusQ9XSM3 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7T6Q_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
EQLSEKRPSTVESGMLSRASVAFQTPSLSRTTSQSSNSHRGWEILRRNDLGHLNLGLDLG
EGDGEEVYHFTETSQVAPA

Ligands and cofactors

IDNameFormulaCopies
PIO[(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-d…C25 H49 O19 P34

Primary citation

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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