8TF3: Wildtype rabbit TRPV5 into nanodiscs

Wildtype rabbit TRPV5 into nanodiscs in complex with econazole. Determined by electron microscopy at 2.94 Å resolution. Released 10 Jan 2024.

Method
Electron microscopy
Resolution
2.94 Å
Organism
Oryctolagus cuniculus
Chains
4
Atoms
19,888
Mol. weight
345.9 kDa
Ligands
CPL, ECN, ERG
Released
10 Jan 2024

Explore 8TF3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8TF3 contains 168 α-helices and 56 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.

Chains A, B, C and D: 42 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix29-4618
α-helix48-558
α-helix58-669
β-strand7511
β-strand8111
α-helix82-887
α-helix92-10110
α-helix103-1075
α-helix1081
β-strand10912
α-helix1101
β-strand11912
α-helix120-1267
α-helix130-1378
α-helix150-1523
α-helix166-1738
α-helix176-1849
α-helix199-2046
α-helix209-22012
α-helix232-2343
α-helix243-2497
α-helix253-2608
β-strand264-27073
β-strand273-27973
α-helix281-2844
α-helix292-2976
α-helix304-3096
α-helix311-32010
α-helix321-3255
α-helix326-34823
β-strand352-35434
β-strand36415
β-strand36616
β-strand368-37034
α-helix371-3722
α-helix380-41031
α-helix412-4176
α-helix423-44422
α-helix451-46313
α-helix464-4718
α-helix476-48510
α-helix486-4905
α-helix491-51222
β-strand51517
α-helix521-5233
α-helix526-53712
α-helix542-5443
β-strand55018
α-helix553-56210
α-helix563-5719
α-helix572-60736
α-helix610-6123
α-helix614-6163
β-strand618-61923
α-helix621-6233
β-strand629-63683

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
>8TF3_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

Ligands and cofactors

IDNameFormulaCopies
CPL1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholineC42 H80 N O8 P8
ECN1-[(2S)-2-[(4-chlorobenzyl)oxy]-2-(2,4-dichlorophenyl)ethyl]-1H-imidazoleC18 H15 Cl3 N2 O4
ERGErgosterolC28 H44 O8

Primary citation

Structural mechanism of TRPV5 inhibition by econazole. De Jesus-Perez, J.J., Gabrielle, M., Raheem, S. et al. Structure (2024) 32:148-156.e5. DOI 10.1016/j.str.2023.11.012 · PubMed

Other PDB entries of the same protein (UniProt Q9XSM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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