9OPU: Constitutively open human TRPC3 mutant

Structure of a constitutively open human TRPC3 mutant. 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: 24,480
Mol. weight: 376.61 kDa
Released: 25 Mar 2026

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

Secondary structure: helices and β-sheets

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.

Chains A, B, C and D: 40 helices, 4 β-strands

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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	820	Homo sapiens	Q13507 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>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

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:

9U5C 2.25 Å, Structure of hTRPC3 in complex with Nb1-94 at 2.25 angstrom
9OLM 2.5 Å, Structure of human TRPC3 cerebellar splice variant (isoform c)
9KDB 2.67 Å, Structure of hTRPC3 in complex with Nb1-25 at 2.67 angstrom
7DXB 2.7 Å, Structure of TRPC3 at 2.7 angstrom in high calcium state
9KDD 2.7 Å, Structure of GSK1702934A-bound TRPC3 at 3.3 angstrom
9VFI 2.72 Å, Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom
9OLK 2.8 Å, Structure of wild-type human TRPC3
9KDC 3.01 Å, Structure of hTRPC3 in complex with Nb3-37 at 3.01 angstrom
7DXC 3.06 Å, Structure of TRPC3 at 3.06 angstrom in low calcium state
9OLL 3.1 Å, Structure of human TRPC3 T573A mutant
7DXE 3.2 Å, Structure of TRPC3 gain of function mutation R803C at 3.2 angstrom in 1340nM free…
6CUD 3.3 Å, Structure of the human TRPC3 in a lipid-occupied, closed state

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