Electron cryo-microscopy structure of the canonical TRPC4 ion channel. Determined by electron microscopy at 3.6 Å resolution. Released 2 May 2018.
Explore 6G1K in 3D Show helices and sheets RCSB PDB PDBe
6G1K contains 152 α-helices and 0 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 | 23-25 | 3 | |
| α-helix | 31-42 | 12 | |
| α-helix | 46-51 | 6 | |
| α-helix | 73-79 | 7 | |
| α-helix | 83-91 | 9 | |
| α-helix | 99-105 | 7 | |
| α-helix | 109-115 | 7 | |
| α-helix | 147-152 | 6 | |
| α-helix | 155-163 | 9 | |
| α-helix | 166-169 | 4 | |
| α-helix | 189-203 | 15 | |
| α-helix | 206-211 | 6 | |
| α-helix | 216-233 | 18 | |
| α-helix | 238-256 | 19 | |
| α-helix | 262-269 | 8 | |
| 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 | 357-360 | 4 | |
| α-helix | 362-381 | 20 | |
| α-helix | 382-384 | 3 | |
| α-helix | 401-422 | 22 | |
| α-helix | 433-456 | 24 | |
| α-helix | 465-467 | 3 | |
| α-helix | 468-469 | 2 | |
| α-helix | 473-490 | 18 | |
| α-helix | 491-495 | 5 | |
| α-helix | 503-538 | 36 | |
| α-helix | 564-573 | 10 | |
| α-helix | 574-576 | 3 | |
| α-helix | 591-606 | 16 | |
| α-helix | 607-612 | 6 | |
| α-helix | 613-625 | 13 | |
| α-helix | 631-644 | 14 | |
| α-helix | 699-724 | 26 | |
| α-helix | 732-750 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily c member 4a | A, B, C, D | protein | 921 | Danio rerio | U3N7D8 (AlphaFold model) |
>6G1K_1 Transient receptor potential cation channel subfamily c member 4a (chains A, B, C, D) GSQLYFRRTDNSSYRDRIPLRIVRAESELSTQEKSYLSAVEKGDYASVKLALEEAEIYFK ININCIDPLGRTALLIAIENENLEIIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKK PSGEKQVPPILLDKQFSDFTPDITPIILAAHTNNYEIIKMLVQKGVSVPQPHEVRCNCVE CVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKAE YEELSHQCKHFAKDLLDQTRSSRELELILNFRDDMNLLQDEANNELARLKLAIKYRQKEF VAQPNCQQLLASRWYDEFPGWRRRHWAGKLITCVFIGLMFPLLSLCYLVAPKSRYGLFIR KPFIKFICHTASYLTFLFLLLLASQHIVSNNPDRQGPKPTTVEWMILPWVLGFIWTEIKQ MWDGGFQDYIHDWWNLMDFVMNSLYLATISLKIVAYVKYSGCKPRDTWEMWHPTLVAEAV FAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFY YENSEGMTCKGIRCERQNNAFSTLFETLQSLFWSIFGLISLYVTNVKADHKFTEFVGATM FGTYNVISLVVLLNMLIAMMNNSYQHIADHADIEWKFARTKLWMSYFEEGGTLPPPFNII PSPKSICYLITWIKVHVFKRRSKRTETFGTLGRRAAENVRLNHQYQEVLRNLVKRYVAAM IRDAKTEEGLTEENFKELKQDISSFRYEVIGMMKGNRKSTRANKSDTSASDVSHPEGSLQ YSSALKQNSKLHLYDVTTALQQQNSEEAKASLGCLANGSAVVLTEPILKDKARSDFPKDF TDFGLFPKKQNPNKIYSLAEEATESDPDILDWGKEDKPLAGKVEQDVNESKCLMEEDERV LEEQEMEHIASSHEHLEVLFQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| 44E | (2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoate | C15 H29 O8 P | 4 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 4 |
Electron cryo-microscopy structure of the canonical TRPC4 ion channel. Vinayagam, D., Mager, T., Apelbaum, A. et al. Elife (2018) 7. DOI 10.7554/eLife.36615 · 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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