Structure of a constitutively open human TRPC3 mutant. Determined by electron microscopy at 3.3 Å resolution. Released 25 Mar 2026.
Explore 9OPU in 3D Show helices and sheets RCSB PDB PDBe
9OPU contains 160 α-helices and 16 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 | 38-48 | 11 | |
| α-helix | 52-60 | 9 | |
| α-helix | 77-83 | 7 | |
| α-helix | 87-94 | 8 | |
| α-helix | 103-112 | 10 | |
| α-helix | 115-122 | 8 | |
| α-helix | 125-128 | 4 | |
| α-helix | 137-143 | 7 | |
| β-strand | 149 | 1 | 1 |
| β-strand | 155 | 1 | 1 |
| α-helix | 163-170 | 8 | |
| α-helix | 173-181 | 9 | |
| α-helix | 189-191 | 3 | |
| α-helix | 197-205 | 9 | |
| α-helix | 208-221 | 14 | |
| α-helix | 224-229 | 6 | |
| α-helix | 234-251 | 18 | |
| α-helix | 256-275 | 20 | |
| α-helix | 280-287 | 8 | |
| α-helix | 307-314 | 8 | |
| α-helix | 324-334 | 11 | |
| α-helix | 341-343 | 3 | |
| α-helix | 346-358 | 13 | |
| α-helix | 361-369 | 9 | |
| α-helix | 373-377 | 5 | |
| α-helix | 382-402 | 21 | |
| α-helix | 427-431 | 5 | |
| α-helix | 436-459 | 24 | |
| α-helix | 469-504 | 36 | |
| α-helix | 510-512 | 3 | |
| α-helix | 534-549 | 16 | |
| α-helix | 552-559 | 8 | |
| α-helix | 563-598 | 36 | |
| β-strand | 606 | 1 | 2 |
| α-helix | 614-623 | 10 | |
| α-helix | 624-626 | 3 | |
| β-strand | 636 | 1 | 2 |
| α-helix | 642-656 | 15 | |
| α-helix | 657-661 | 5 | |
| α-helix | 662-674 | 13 | |
| α-helix | 681-694 | 14 | |
| α-helix | 705-707 | 3 | |
| α-helix | 746-795 | 22 | |
| α-helix | 801-837 | 37 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Short transient receptor potential channel 3 | A, B, C, D | protein | 820 | Homo sapiens | Q13507 (AlphaFold model) |
>9OPU_1 Short transient receptor potential channel 3 (chains A, B, C, D) MEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLE ESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEA ILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLL MKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALE LSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVH RHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGL PFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVT DYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIF IAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEG LYAIAVVLSFSRIAYILPANESFGPLQISLGRAVKDIFKFMVLFIMVFFAFMIGMFILYS YYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVV VLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFI MRIVNFPKCRRRRLQKDIEMGMGNSKSRQIMKRLIKRYVLKAQVDKENDEVNEGELKEIK QDISSLRYELLEDKSQATEELAILIHKLSEISSLRYELLE
Functional and structural basis of a hypermorphic TRPC3 variant. Bell, B., Jaramillo-Granada, A.M., Romero, L.O. et al. Sci Adv (2026) 12:eaec9284-eaec9284. DOI 10.1126/sciadv.aec9284 · PubMed
Other PDB entries of the same protein (UniProt Q13507 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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