9U5C: HTRPC3

Structure of hTRPC3 in complex with Nb1-94 at 2.25 angstrom. Determined by electron microscopy at 2.25 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.25 Å
Organisms: Homo sapiens, Camelus
Chains: 8
Atoms: 27,616
Mol. weight: 443.77 kDa
Ligands: A1L5I, ZN, CA
Released: 8 Oct 2025

Explore 9U5C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9U5C contains 192 α-helices and 84 β-strands across 8 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, C, E and G: 46 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	26-36	11
α-helix	40-49	10
β-strand	58	1	1
β-strand	64	1	1
α-helix	65-71	7
α-helix	75-81	7
α-helix	90-100	11
α-helix	103-110	8
α-helix	113-116	4
α-helix	120-122	3
α-helix	125-130	6
β-strand	137	1	2
β-strand	143	1	2
α-helix	151-157	7
α-helix	161-169	9
α-helix	174-179	6
α-helix	185-193	9
α-helix	195-209	15
α-helix	212-218	7
α-helix	222-239	18
α-helix	244-263	20
α-helix	268-276	9
α-helix	295-302	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	334-346	13
α-helix	348-357	10
α-helix	362-367	6
α-helix	370-391	22
α-helix	393-395	3
α-helix	415-420	6
α-helix	421-423	3
α-helix	424-447	24
α-helix	449-452	4
α-helix	456-492	37
α-helix	505-508	4
α-helix	509-511	3
α-helix	514-516	3
α-helix	522-537	16
α-helix	540-543	4
α-helix	545-547	3
α-helix	552-587	36
α-helix	588-590	3
β-strand	594	1	3
α-helix	602-611	10
α-helix	619-622	4
β-strand	624	1	3
α-helix	629-658	30
α-helix	668-683	16
α-helix	762-783	22
β-strand	786	1	4
α-helix	787	1
β-strand	788	1	5
α-helix	789-828	40

Chains B, D, F and H: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	6
β-strand	11	1	7
β-strand	18-26	9	6
α-helix	31-33	3
β-strand	35-41	7	8
β-strand	47-53	7	8
β-strand	59-61	3	8
β-strand	70-74	5	6
β-strand	79-84	6	6
β-strand	93-95	3	9
β-strand	96-100	5	8
α-helix	113-117	5
β-strand	120-121	2	8
β-strand	125-127	3	9
β-strand	128	1	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, C, E, G	protein	836	Homo sapiens	Q13507 (AlphaFold model)
Nb1-94	B, D, F, H	protein	129	Camelus

Sequence of entity 1 (A, C, E, G), FASTA

>9U5C_1 Short transient receptor potential channel 3 (chains A, C, E, G)
MREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLEESKTLNVNCVDY
MGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEAILNHPGFAASKR
LTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLLMKGARIERPHDY
FCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALELSNELAKLANIE
KEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVHRHKASLSRVKLA
IKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGLPFLAIGYWIAPC
SRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVTDYPKQIFRVKTT
QFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIFIAAFTARFLAFL
QATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEGLYAIAVVLSFSR
IAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFFAFMIGMFILYSYYLGAKVNAAFT
TVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVVVLLNMLIAMINS
SYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFIMRIVNFPKCRRR
RLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMKRLIKRYVLKAQV
DKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKLNPSMLRCE

Sequence of entity 2 (B, D, F, H), FASTA

>9U5C_2 Nb1-94 (chains B, D, F, H)
QVQLQESGGGSVQSGGSLRLSCAASGYTYSYSGYCMGWFRQAPGKEREGVATIDGAGNTK
YADSVKGRFTISRDNAKKTLYLQMNSLKPEDTAMYYCAARVYSYSSDVDCRPSFTTRFPY
SGQGTQVTV

Ligands and cofactors

ID	Name	Formula	Copies
A1L5I	[(2~{S})-2-[(~{E})-octadec-9-enoyl]oxy-3-oxidanyl-propyl] octadec-9-enoate	C39 H72 O5	4
ZN	Zinc ion	Zn	4
CA	Calcium ion	Ca	8

Primary citation

Structural mechanism of the agonist binding on human TRPC3 channel. Chen, Y., Zang, J., Guo, W. et al. Nat Commun (2025) 16:9343-9343. DOI 10.1038/s41467-025-64435-6 · PubMed

Other PDB entries of the same protein (UniProt Q13507 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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
9OLX 3.3 Å, Structure of a constitutively open human TRPC3 mutant in the inhibited state

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