9KDD: GSK1702934A-bound TRPC3

Structure of GSK1702934A-bound TRPC3 at 3.3 angstrom. Determined by electron microscopy at 2.7 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 21,624
Mol. weight: 424.49 kDa
Ligands: A1L5P, ZN
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9KDD contains 163 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 and C: 41 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	26-36	11
α-helix	40-46	7
β-strand	58	1	1
β-strand	64	1	1
α-helix	65-71	7
α-helix	75-82	8
α-helix	90-99	10
α-helix	103-110	8
α-helix	113-116	4
α-helix	151-158	8
α-helix	161-169	9
α-helix	174-177	4
α-helix	185-192	8
α-helix	195-209	15
α-helix	212-218	7
α-helix	222-240	19
α-helix	244-263	20
α-helix	268-275	8
α-helix	295-302	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	328-331	4
α-helix	334-354	21
α-helix	358-360	3
α-helix	362-367	6
α-helix	370-391	22
α-helix	415-420	6
α-helix	421-423	3
α-helix	424-447	24
α-helix	449-453	5
α-helix	456-491	36
α-helix	505-508	4
α-helix	509-511	3
α-helix	522-537	16
α-helix	538-543	6
α-helix	545-547	3
α-helix	552-587	36
β-strand	594	1	2
α-helix	602-611	10
α-helix	619-622	4
β-strand	624	1	2
α-helix	629-660	32
α-helix	668-685	18
α-helix	693-696	4
α-helix	762-786	25

Chain D: 40 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	26-36	11
α-helix	40-46	7
β-strand	58	1	7
β-strand	64	1	7
α-helix	65-71	7
α-helix	75-82	8
α-helix	90-99	10
α-helix	103-110	8
α-helix	113-116	4
α-helix	151-158	8
α-helix	161-169	9
α-helix	174-177	4
α-helix	185-192	8
α-helix	195-209	15
α-helix	212-218	7
α-helix	222-240	19
α-helix	244-263	20
α-helix	268-275	8
α-helix	295-302	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	328-331	4
α-helix	334-354	21
α-helix	358-360	3
α-helix	362-367	6
α-helix	370-391	22
α-helix	415-420	6
α-helix	424-447	24
α-helix	449-453	5
α-helix	456-491	36
α-helix	505-508	4
α-helix	509-511	3
α-helix	522-537	16
α-helix	538-543	6
α-helix	545-547	3
α-helix	552-587	36
β-strand	594	1	8
α-helix	602-611	10
α-helix	619-622	4
β-strand	624	1	8
α-helix	629-660	32
α-helix	668-685	18
α-helix	693-696	4
α-helix	762-786	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	921	Homo sapiens	Q13507 (AlphaFold model)

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

>9KDD_1 Short transient receptor potential channel 3 (chains A, B, C, D)
MSTKVRKCKEQARVTFPAPEEEEDEGEDEGAEPQRRRRGWRGVNGGLEPRSAPSQREPHG
YCPPPFSHGPDLSMEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAA
EYGNIPVVRKMLEESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALL
LAISKGYVRIVEAILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILA
AHCQKYEVVHMLLMKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYL
SLSSEDPVLTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAIL
NGDLESAEPLEVHRHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIA
IKCLVVLVVALGLPFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDR
FEGITTLPNITVTDYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQ
LWNVLDFGMLSIFIAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARD
KWLPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMV
FFAFMIGMFILYSYYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIG
YVLYGIYNVTMVVVLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPF
SLVPSPKSFVYFIMRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNS
ILNQPTRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATE
ELAILIHKLSEKLNPSMLRCE

Ligands and cofactors

ID	Name	Formula	Copies
A1L5P	3-[1-(5,6,7,8-tetrahydro-4~{H}-cyclohepta[b]thiophen-2-ylcarbonyl)piperidin-4-y…	C22 H25 N3 O2 S	4
ZN	Zinc ion	Zn	4

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:

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
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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