TRPC4 in complex with E-AzPico. Determined by electron microscopy at 3.0 Å resolution. Released 9 Jul 2025.
Explore 9FXL in 3D Show helices and sheets RCSB PDB PDBe
9FXL contains 161 α-helices and 10 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 |
|---|---|---|---|
| β-strand | 20 | 1 | 1 |
| α-helix | 33-42 | 10 | |
| α-helix | 45-52 | 8 | |
| β-strand | 66 | 1 | 2 |
| β-strand | 72 | 1 | 2 |
| α-helix | 73-80 | 8 | |
| α-helix | 83-91 | 9 | |
| α-helix | 99-105 | 7 | |
| α-helix | 110-116 | 7 | |
| α-helix | 145-152 | 8 | |
| α-helix | 155-164 | 10 | |
| α-helix | 169-171 | 3 | |
| α-helix | 189-203 | 15 | |
| α-helix | 206-212 | 7 | |
| α-helix | 218-233 | 16 | |
| α-helix | 235-237 | 3 | |
| α-helix | 239-256 | 18 | |
| α-helix | 262-268 | 7 | |
| α-helix | 289-294 | 6 | |
| α-helix | 298-301 | 4 | |
| α-helix | 304-315 | 12 | |
| α-helix | 326-338 | 13 | |
| α-helix | 342-349 | 8 | |
| α-helix | 362-381 | 20 | |
| α-helix | 397-399 | 3 | |
| α-helix | 401-424 | 24 | |
| α-helix | 433-454 | 22 | |
| α-helix | 469 | 1 | |
| α-helix | 473-490 | 18 | |
| α-helix | 491-496 | 6 | |
| α-helix | 502-510 | 9 | |
| α-helix | 516-538 | 23 | |
| α-helix | 539-541 | 3 | |
| α-helix | 564-572 | 9 | |
| α-helix | 581-584 | 4 | |
| α-helix | 591-605 | 15 | |
| α-helix | 606-612 | 7 | |
| α-helix | 613-627 | 15 | |
| α-helix | 631-643 | 13 | |
| α-helix | 700-720 | 21 | |
| α-helix | 722-725 | 4 | |
| α-helix | 733-752 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-42 | 10 | |
| α-helix | 45-51 | 7 | |
| β-strand | 66 | 1 | 3 |
| β-strand | 72 | 1 | 3 |
| α-helix | 73-79 | 7 | |
| α-helix | 83-91 | 9 | |
| α-helix | 99-106 | 8 | |
| α-helix | 109-115 | 7 | |
| α-helix | 145-152 | 8 | |
| α-helix | 155-164 | 10 | |
| β-strand | 167 | 1 | 4 |
| α-helix | 168-170 | 3 | |
| α-helix | 189-203 | 15 | |
| α-helix | 206-212 | 7 | |
| α-helix | 216-230 | 15 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-256 | 19 | |
| α-helix | 262-268 | 7 | |
| α-helix | 287-294 | 8 | |
| α-helix | 298-301 | 4 | |
| α-helix | 304-315 | 12 | |
| α-helix | 326-338 | 13 | |
| α-helix | 345-349 | 5 | |
| α-helix | 362-381 | 20 | |
| α-helix | 382-384 | 3 | |
| α-helix | 397-399 | 3 | |
| α-helix | 401-421 | 21 | |
| α-helix | 433-458 | 26 | |
| α-helix | 465-467 | 3 | |
| α-helix | 468-469 | 2 | |
| α-helix | 473-490 | 18 | |
| α-helix | 491-498 | 8 | |
| α-helix | 502-511 | 10 | |
| α-helix | 513-538 | 26 | |
| α-helix | 564-570 | 7 | |
| α-helix | 581-584 | 4 | |
| α-helix | 591-606 | 16 | |
| α-helix | 607-612 | 6 | |
| α-helix | 617-627 | 11 | |
| α-helix | 631-644 | 14 | |
| α-helix | 655-657 | 3 | |
| α-helix | 699-721 | 23 | |
| α-helix | 732-752 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20 | 1 | 4 |
| α-helix | 33-42 | 10 | |
| α-helix | 45-52 | 8 | |
| α-helix | 73-79 | 7 | |
| α-helix | 83-91 | 9 | |
| α-helix | 99-106 | 8 | |
| α-helix | 109-116 | 8 | |
| α-helix | 145-152 | 8 | |
| α-helix | 155-164 | 10 | |
| α-helix | 168-171 | 4 | |
| α-helix | 189-203 | 15 | |
| α-helix | 206-211 | 6 | |
| α-helix | 216-226 | 11 | |
| α-helix | 230-233 | 4 | |
| α-helix | 239-256 | 18 | |
| α-helix | 262-268 | 7 | |
| α-helix | 287-294 | 8 | |
| α-helix | 298-301 | 4 | |
| α-helix | 304-315 | 12 | |
| α-helix | 326-337 | 12 | |
| α-helix | 340-349 | 10 | |
| α-helix | 362-381 | 20 | |
| α-helix | 382-384 | 3 | |
| α-helix | 397-399 | 3 | |
| α-helix | 401-421 | 21 | |
| α-helix | 433-457 | 25 | |
| α-helix | 465-467 | 3 | |
| α-helix | 473-489 | 17 | |
| α-helix | 492-496 | 5 | |
| α-helix | 502-509 | 8 | |
| α-helix | 514-538 | 25 | |
| α-helix | 539-541 | 3 | |
| α-helix | 564-572 | 9 | |
| α-helix | 581-584 | 4 | |
| α-helix | 591-606 | 16 | |
| α-helix | 607-611 | 5 | |
| α-helix | 614-627 | 14 | |
| α-helix | 628-630 | 3 | |
| α-helix | 632-643 | 12 | |
| α-helix | 644-646 | 3 | |
| α-helix | 701-726 | 26 | |
| α-helix | 732-752 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-41 | 9 | |
| α-helix | 46-54 | 9 | |
| α-helix | 73-79 | 7 | |
| α-helix | 83-91 | 9 | |
| α-helix | 99-105 | 7 | |
| α-helix | 109-116 | 8 | |
| α-helix | 145-152 | 8 | |
| α-helix | 155-164 | 10 | |
| β-strand | 167 | 1 | 1 |
| α-helix | 169-171 | 3 | |
| α-helix | 189-193 | 5 | |
| α-helix | 197-203 | 7 | |
| α-helix | 206-211 | 6 | |
| α-helix | 216-232 | 17 | |
| α-helix | 238-256 | 19 | |
| α-helix | 262-268 | 7 | |
| α-helix | 287-294 | 8 | |
| α-helix | 298-301 | 4 | |
| α-helix | 304-314 | 11 | |
| α-helix | 326-338 | 13 | |
| α-helix | 340-349 | 10 | |
| α-helix | 362-382 | 21 | |
| β-strand | 394 | 1 | 5 |
| α-helix | 397-399 | 3 | |
| α-helix | 401-424 | 24 | |
| α-helix | 433-457 | 25 | |
| β-strand | 462 | 1 | 5 |
| α-helix | 465-467 | 3 | |
| α-helix | 468-469 | 2 | |
| α-helix | 473-490 | 18 | |
| α-helix | 491-498 | 8 | |
| α-helix | 502-511 | 10 | |
| α-helix | 513-538 | 26 | |
| α-helix | 539-541 | 3 | |
| α-helix | 564-573 | 10 | |
| α-helix | 574-576 | 3 | |
| α-helix | 581-584 | 4 | |
| α-helix | 591-605 | 15 | |
| α-helix | 606-610 | 5 | |
| α-helix | 615-627 | 13 | |
| α-helix | 632-644 | 13 | |
| α-helix | 702-725 | 24 | |
| α-helix | 733-735 | 3 | |
| α-helix | 736-752 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily c member 4a | A, B, C, D | protein | 941 | Danio rerio | U3N7D8 (AlphaFold model) |
>9FXL_1 Transient receptor potential cation channel subfamily c member 4a (chains A, B, C, D) MGHHHHHHHHGGSENLYFQGGSQLYFRRTDNSSYRDRIPLRIVRAESELSTQEKSYLSAV EKGDYASVKLALEEAEIYFKININCIDPLGRTALLIAIENENLEIIELLLSFNVYVGDAL LHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSDFTPDITPIILAAHTNNYEIIKM LVQKGVSVPQPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTA FQLSWELQELSKVENEFKAEYEELSHQCKHFAKDLLDQTRSSRELELILNFRDDMNLLQD EANNELARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWAGKLITCVFIGLMF PLLSLCYLVAPKSRYGLFIRKPFIKFICHTASYLTFLFLLLLASQHIVSNNPDRQGPKPT TVEWMILPWVLGFIWTEIKQMWDGGFQDYIHDWWNLMDFVMNSLYLATISLKIVAYVKYS GCKPRDTWEMWHPTLVAEAVFAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFL FIYCLVLLAFANGLNQLYFYYENSEGMTCKGIRCERQNNAFSTLFETLQSLFWSIFGLIS LYVTNVKADHKFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQHIADHADIEWKFART KLWMSYFEEGGTLPPPFNIIPSPKSICYLITWIKVHVFKRRSKRTETFGTLGRRAAENVR LNHQYQEVLRNLVKRYVAAMIRDAKTEEGLTEENFKELKQDISSFRYEVIGMMKGNRKST RANKSDTSASDVSHPEGSLQYSSALKQNSKLHLYDVTTALQQQNSEEAKASLGCLANGSA VVLTEPILKDKARSDFPKDFTDFGLFPKKQNPNKIYSLAEEATESDPDILDWGKEDKPLA GKVEQDVNESKCLMEEDERVLEEQEMEHIASSHEHLEVLFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1IGW | (E)-7-(4-chlorobenzyl)-1-(3-hydroxypropyl)-3-methyl-8-(4-(phenyldiazenyl)-3-(tr… | C29 H24 Cl F3 N6 O5 | 4 |
Ideal efficacy photoswitching for chromocontrol of TRPC4/5 channel functions in live tissues. Muller, M., Niemeyer, K., Ojha, N.K. et al. Nat Chem Biol (2026) 22:180-191. DOI 10.1038/s41589-025-02085-x · PubMed
Other PDB entries of the same protein (UniProt U3N7D8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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