Structure of GSK1702934A-bound TRPC3 at 3.3 angstrom. Determined by electron microscopy at 2.7 Å resolution. Released 8 Oct 2025.
Explore 9KDD in 3D Show helices and sheets RCSB PDB PDBe
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.
| 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 |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Short transient receptor potential channel 3 | A, B, C, D | protein | 921 | Homo sapiens | Q13507 (AlphaFold model) |
>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
| 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 |
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:
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