8FHI: Wildtype rabbit TRPV5 in nanodiscs

Wildtype rabbit TRPV5 in nanodiscs in complex with oleoyl coenzyme A, Open stated. Determined by electron microscopy at 3.25 Å resolution. Released 1 Nov 2023.

Method
Electron microscopy
Resolution
3.25 Å
Organism
Oryctolagus cuniculus
Chains
4
Atoms
20,116
Mol. weight
345.48 kDa
Ligands
POV, 3VV, ERG
Released
1 Nov 2023

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

Secondary structure: helices and β-sheets

8FHI 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-helix30-4617
α-helix48-558
α-helix58-669
α-helix82-887
α-helix92-1009
α-helix103-1075
α-helix113-1153
α-helix120-1267
α-helix130-1389
α-helix166-1738
α-helix176-1849
α-helix199-2046
α-helix210-22112
α-helix232-2343
α-helix243-2497
α-helix253-2619
β-strand264-27071
β-strand273-27971
α-helix292-2976
α-helix302-3098
α-helix311-32010
α-helix321-3255
α-helix326-34823
β-strand352-35432
β-strand36413
β-strand368-37032
α-helix371-3722
α-helix380-40930
α-helix412-4165
α-helix424-44421
α-helix451-46313
α-helix464-4718
α-helix476-48510
α-helix486-4905
α-helix491-51121
α-helix521-5233
α-helix526-53712
β-strand55014
α-helix553-56210
α-helix563-5708
α-helix571-58616
α-helix589-60719
α-helix610-6123
α-helix614-6163
β-strand61811
β-strand630-63671

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
>8FHI_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
POV(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…C42 H82 N O8 P4
3VVS-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphono…C39 H68 N7 O17 P3 S4
ERGErgosterolC28 H44 O8

Primary citation

Structural basis of the activation of TRPV5 channels by long-chain acyl-Coenzyme-A. Lee, B.H., De Jesus Perez, J.J., Moiseenkova-Bell, V. et al. Nat Commun (2023) 14:5883-5883. DOI 10.1038/s41467-023-41577-z · 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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