9BKU: TRPV3 K169A in nanodiscs incubated with NASPM

Cryo-EM structure of TRPV3 K169A in nanodiscs incubated with NASPM. Determined by electron microscopy at 3.39 Å resolution. Released 21 May 2025.

Method
Electron microscopy
Resolution
3.39 Å
Organism
Homo sapiens
Chains
4
Atoms
17,504
Mol. weight
392.6 kDa
Ligands
6OU
Released
21 May 2025

Explore 9BKU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9BKU 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-helix132-14615
α-helix159-1624
β-strand16411
β-strand16911
α-helix171-1777
α-helix183-19614
α-helix200-2045
α-helix218-2247
α-helix228-2369
α-helix255-2573
α-helix265-2717
α-helix275-2839
α-helix299-3068
α-helix316-32813
α-helix332-3354
α-helix344-3518
α-helix354-3618
α-helix371-3733
β-strand376-38272
β-strand385-39172
α-helix403-4097
α-helix416-4205
α-helix426-4327
α-helix433-4375
α-helix438-46023
α-helix483-50725
α-helix521-54121
α-helix547-56014
α-helix561-5677
α-helix570-58213
α-helix583-5875
α-helix588-60619
β-strand60913
α-helix625-63713
β-strand64813
α-helix651-66212
α-helix663-6708
α-helix671-68515
α-helix689-70618
α-helix709-7157
β-strand719-72022
β-strand730-73782
α-helix739-7468

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily V member 3A, B, C, Dprotein799Homo sapiensQ8NET8 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9BKU_1 Transient receptor potential cation channel subfamily V member 3 (chains A, B, C, D)
MKAHPKEMVPLMGKRVAAPSGNPAVLPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTS
PPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLK
KRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGATCLMKALLNIN
PNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGAD
VNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNIL
HALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYI
LSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEML
TLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMG
WLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLY
LFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLG
FGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLIT
YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGEL
CKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAFE
EVEEFPETSVSNSLEVLFQ

Ligands and cofactors

IDNameFormulaCopies
6OU[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y…C39 H76 N O8 P36

Primary citation

Molecular basis of TRPV3 channel blockade by intracellular polyamines. Zhang, J., Yuan, P., Nichols, C.G. et al. Commun Biol (2025) 8:727-727. DOI 10.1038/s42003-025-08103-x · 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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