Structure of human TRPC3 T573A mutant. Determined by electron microscopy at 3.1 Å resolution. Released 25 Mar 2026.
Explore 9OLL in 3D Show helices and sheets RCSB PDB PDBe
9OLL contains 168 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 | 35-37 | 3 | |
| α-helix | 38-49 | 12 | |
| α-helix | 52-61 | 10 | |
| 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 | 149-151 | 3 | 1 |
| β-strand | 154-155 | 2 | 1 |
| α-helix | 163-170 | 8 | |
| α-helix | 173-180 | 8 | |
| α-helix | 187-189 | 3 | |
| α-helix | 197-204 | 8 | |
| α-helix | 207-221 | 15 | |
| α-helix | 224-230 | 7 | |
| α-helix | 234-251 | 18 | |
| α-helix | 256-275 | 20 | |
| α-helix | 280-288 | 9 | |
| α-helix | 307-315 | 9 | |
| α-helix | 318-321 | 4 | |
| α-helix | 324-334 | 11 | |
| α-helix | 349-358 | 10 | |
| α-helix | 360-369 | 10 | |
| α-helix | 374-380 | 7 | |
| α-helix | 382-402 | 21 | |
| α-helix | 427-431 | 5 | |
| α-helix | 436-458 | 23 | |
| α-helix | 461-464 | 4 | |
| α-helix | 470-504 | 35 | |
| α-helix | 517-520 | 4 | |
| α-helix | 521-523 | 3 | |
| α-helix | 526-528 | 3 | |
| α-helix | 534-549 | 16 | |
| α-helix | 552-555 | 4 | |
| α-helix | 557-559 | 3 | |
| α-helix | 563-599 | 37 | |
| β-strand | 606 | 1 | 2 |
| α-helix | 614-622 | 9 | |
| α-helix | 631-633 | 3 | |
| β-strand | 636 | 1 | 2 |
| α-helix | 641-675 | 35 | |
| α-helix | 680-693 | 14 | |
| α-helix | 774-795 | 22 | |
| α-helix | 801-836 | 36 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Short transient receptor potential channel 3 | A, B, C, D | protein | 848 | Homo sapiens | Q13507 (AlphaFold model) |
>9OLL_1 Short transient receptor potential channel 3 (chains A, B, C, D) MEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLE ESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEA ILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLL MKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALE LSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVH RHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGL PFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVT DYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIF IAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEG LYAIAVVLSFSRIAYILPANESFGPLQISLGRAVKDIFKFMVLFIMVFFAFMIGMFILYS YYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVV VLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFI MRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMK RLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKL NPSMLRCE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CPL | 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine | C42 H80 N O8 P | 12 |
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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