9PJ5: PDB entry 9PJ5

Closed-state structure of wild-type human TRPV3 purified in GDN detergent. Determined by electron microscopy at 2.76 Å resolution. Released 1 Jul 2026.

Method
Electron microscopy
Resolution
2.76 Å
Organism
Homo sapiens
Chains
4
Atoms
22,278
Mol. weight
395.09 kDa
Ligands
POV
Released
1 Jul 2026

Explore 9PJ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PJ5 contains 140 α-helices and 40 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: 35 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix120-12910
α-helix132-14615
α-helix155-1584
β-strand16311
β-strand17011
α-helix171-1777
α-helix183-19614
α-helix200-2034
β-strand20812
β-strand21412
α-helix218-2247
α-helix228-23710
α-helix265-2717
α-helix275-2828
α-helix299-3057
α-helix316-32813
α-helix332-3354
α-helix344-3507
α-helix354-3618
α-helix371-3733
β-strand376-38273
β-strand385-39173
α-helix403-4086
α-helix416-4194
α-helix423-43210
α-helix433-4375
α-helix438-46023
α-helix482-50625
α-helix521-54121
α-helix547-56014
α-helix561-5688
α-helix570-58213
α-helix583-5875
α-helix588-60720
β-strand60914
α-helix610-6123
α-helix625-63713
β-strand64814
α-helix651-66212
α-helix663-6697
α-helix670-68415
α-helix688-70619
α-helix709-7124
β-strand719-72463
β-strand727-737113

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
>9PJ5_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
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

Structural diversity of heat-sensing channel TRPV3 with Olmsted syndrome mutations. Khau, J., Purohit, R., Nadezhdin, K.D. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-74687-5 · 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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