9OLX: Short transient receptor potential channel 3

Structure of a constitutively open human TRPC3 mutant in the inhibited state. Determined by electron microscopy at 3.3 Å resolution. Released 25 Mar 2026.

Method
Electron microscopy
Resolution
3.3 Å
Organism
Homo sapiens
Chains
4
Atoms
24,592
Mol. weight
382.46 kDa
Ligands
A1CCX
Released
25 Mar 2026

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

Secondary structure: helices and β-sheets

9OLX contains 168 α-helices and 24 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: 42 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix36-427
α-helix43-475
α-helix52-598
β-strand8111
β-strand8411
α-helix87-959
α-helix102-11211
α-helix115-1228
α-helix125-1284
α-helix137-1437
β-strand14912
β-strand15512
α-helix163-1708
α-helix173-1819
α-helix197-2059
α-helix209-22113
α-helix226-2294
α-helix234-25017
α-helix257-27014
α-helix280-2878
α-helix308-3147
α-helix319-3224
α-helix324-33512
α-helix339-3413
α-helix346-36924
α-helix373-3786
α-helix382-40221
α-helix427-4315
α-helix433-4353
α-helix436-45823
α-helix461-4644
α-helix469-50335
α-helix517-5204
α-helix521-5233
α-helix526-5283
α-helix534-54815
α-helix551-5555
α-helix557-5593
α-helix564-59835
β-strand60613
α-helix614-6229
α-helix631-6333
β-strand63613
α-helix641-67535
α-helix680-69718
α-helix705-7073
α-helix744-79423
α-helix802-83736

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Short transient receptor potential channel 3A, B, C, Dprotein820Homo sapiensQ13507 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9OLX_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

Ligands and cofactors

IDNameFormulaCopies
A1CCX(3,4-dihydroisoquinolin-2(1H)-yl)[2-(4-methoxyanilino)-1,3-thiazol-4-yl]methano…C20 H19 N3 O2 S4

Water and common crystallization additives (UNL) are not listed.

Primary citation

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:

Browse structure collections

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