8V6O: PDB entry 8V6O

Inactivated-state cryo-EM structure of human TRPV3 in presence of 2-APB in cNW30 nanodiscs. Determined by electron microscopy at 2.83 Å resolution. Released 17 Apr 2024.

Method
Electron microscopy
Resolution
2.83 Å
Organism
Homo sapiens
Chains
4
Atoms
22,683
Mol. weight
396.91 kDa
Ligands
FZ4, POV
Released
17 Apr 2024

Explore 8V6O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8V6O contains 144 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: 36 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix118-12912
α-helix132-14413
α-helix154-1629
α-helix171-1777
α-helix185-19612
α-helix200-2045
β-strand20811
β-strand21411
α-helix218-2247
α-helix228-23710
α-helix265-2717
α-helix275-2839
α-helix299-3057
α-helix316-32813
α-helix344-3518
α-helix354-3618
α-helix371-3733
β-strand376-38272
β-strand385-39172
α-helix403-4086
α-helix416-4194
α-helix423-43210
α-helix433-4375
α-helix438-45720
α-helix470-4712
α-helix481-50424
α-helix516-5194
α-helix522-54120
α-helix547-56014
α-helix561-5688
α-helix570-58112
α-helix582-5865
α-helix587-60519
β-strand60913
α-helix610-6112
α-helix612-6143
α-helix624-63714
α-helix643-6464
β-strand64813
α-helix651-67626
α-helix682-70625
α-helix709-7124
β-strand719-72462
β-strand727-737112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 3A, B, C, Dprotein808Homo sapiensQ8NET8 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>8V6O_1 Transient receptor potential cation channel subfamily V member 3 (chains A, B, C, D)
MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTS
PPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLK
KRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNIN
PNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGAD
VNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNIL
HALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYI
LSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEML
TLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMG
WLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLY
LFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLG
FGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLIT
YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGEL
CKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTADFNKIQDSSRNNSKTTLNAF
EEVEEFPETSVLVPRGSAAAWSHPQFEK

Ligands and cofactors

IDNameFormulaCopies
FZ42-aminoethyl diphenylborinateC14 H16 B N O8
POV(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…C42 H82 N O8 P32

Water and common crystallization additives (NA) are not listed.

Primary citation

TRPV3 activation by different agonists accompanied by lipid dissociation from the vanilloid site. Nadezhdin, K.D., Neuberger, A., Khosrof, L.S. et al. Sci Adv (2024) 10:eadn2453-eadn2453. DOI 10.1126/sciadv.adn2453 · PubMed

Other PDB entries of the same protein (UniProt Q8NET8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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