Structure of human TRPV3-G568C Olmsted syndrome mutant in the closed state. Determined by electron microscopy at 2.86 Å resolution. Released 1 Jul 2026.
Explore 13LJ in 3D Show helices and sheets RCSB PDB PDBe
13LJ 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 120-129 | 10 | |
| α-helix | 132-145 | 14 | |
| α-helix | 146-148 | 3 | |
| α-helix | 154-160 | 7 | |
| β-strand | 163 | 1 | 1 |
| β-strand | 170 | 1 | 1 |
| α-helix | 171-177 | 7 | |
| α-helix | 183-194 | 12 | |
| α-helix | 200-203 | 4 | |
| α-helix | 218-224 | 7 | |
| α-helix | 228-237 | 10 | |
| α-helix | 265-271 | 7 | |
| α-helix | 275-282 | 8 | |
| α-helix | 299-306 | 8 | |
| α-helix | 316-328 | 13 | |
| α-helix | 332-335 | 4 | |
| α-helix | 344-350 | 7 | |
| α-helix | 354-361 | 8 | |
| α-helix | 371-373 | 3 | |
| β-strand | 376-382 | 7 | 2 |
| β-strand | 385-391 | 7 | 2 |
| α-helix | 403-408 | 6 | |
| α-helix | 416-418 | 3 | |
| α-helix | 423-432 | 10 | |
| α-helix | 433-437 | 5 | |
| α-helix | 440-460 | 21 | |
| α-helix | 483-487 | 5 | |
| α-helix | 489-492 | 4 | |
| α-helix | 495-506 | 12 | |
| α-helix | 516-519 | 4 | |
| α-helix | 521-541 | 21 | |
| α-helix | 547-560 | 14 | |
| α-helix | 570-582 | 13 | |
| α-helix | 583-587 | 5 | |
| α-helix | 588-607 | 20 | |
| β-strand | 609 | 1 | 3 |
| α-helix | 610-611 | 2 | |
| α-helix | 625-636 | 12 | |
| β-strand | 648 | 1 | 3 |
| α-helix | 651-662 | 12 | |
| α-helix | 663-669 | 7 | |
| α-helix | 670-684 | 15 | |
| α-helix | 688-704 | 17 | |
| α-helix | 709-712 | 4 | |
| β-strand | 719-724 | 6 | 2 |
| β-strand | 727-737 | 11 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 2 of Transient receptor potential cation channel subfamily V member 3,Green fluorescent… | A, B, C, D | protein | 1052 | Homo sapiens, Aequorea victoria | P42212 (AlphaFold model), Q8NET8 (AlphaFold model) |
>13LJ_1 Isoform 2 of Transient receptor potential cation channel subfamily V member 3,Green fluorescent protein (chains A, B, C, D) MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTS PPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLK KRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNIN PNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGAD VNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNIL HALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYI LSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEML TLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMG WLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLY LFAYKEYLACLVLAMALGWANMLYYTRCFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLG FGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLIT YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGEL CKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTADFNKIQDSSRNNSKTTLNAF EEVEEFPETSVLVPRGSAAAAVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATY GKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIF FKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKN GIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSKLSKDPNEKRDHMV LLEFVTAAGITLGMDELYKSGLRSWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 32 |
Water and common crystallization additives (NA) are not listed.
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 P42212 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 13LJ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.