8FFN: RR-bound wildtype rabbit TRPV5 in nanodiscs

RR-bound wildtype rabbit TRPV5 in nanodiscs. Determined by electron microscopy at 2.96 Å resolution. Released 7 Feb 2024.

Method
Electron microscopy
Resolution
2.96 Å
Organism
Oryctolagus cuniculus
Chains
4
Atoms
19,871
Mol. weight
344.97 kDa
Ligands
R2R, POV, ERG
Released
7 Feb 2024

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

Secondary structure: helices and β-sheets

8FFN 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.

Chains A, B, C and D: 38 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix29-4618
α-helix48-547
α-helix58-669
α-helix82-887
α-helix92-10110
α-helix103-1064
α-helix113-1153
α-helix120-1267
α-helix130-13910
α-helix166-1738
α-helix176-1849
α-helix199-2046
α-helix211-22111
α-helix232-2343
α-helix235-2373
α-helix243-2508
α-helix253-2597
β-strand266-27051
β-strand273-27971
α-helix281-2844
α-helix292-2976
α-helix302-3098
α-helix313-3208
α-helix321-3255
α-helix326-34823
β-strand352-35432
β-strand36613
β-strand368-37032
α-helix373-3764
α-helix380-41031
α-helix412-4176
α-helix423-44523
α-helix451-46313
α-helix464-4718
α-helix476-48611
α-helix489-51123
β-strand51514
α-helix526-53712
α-helix553-56210
α-helix563-5708
α-helix571-58414
α-helix586-60722
α-helix610-6123
α-helix614-6163
β-strand618-61921
β-strand629-63681

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
>8FFN_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
R2Rruthenium(6+) azanide pentaamino(oxido)ruthenium (1/4/2)H42 N14 O2 Ru31
POV(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…C42 H82 N O8 P8
ERGErgosterolC28 H44 O8

Primary citation

Molecular details of ruthenium red pore block in TRPV channels. Pumroy, R.A., De Jesus-Perez, J.J., Protopopova, A.D. et al. EMBO Rep (2024) 25:506-523. DOI 10.1038/s44319-023-00050-0 · 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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