Structure of the mouse TRPC4 ion channel. Determined by electron microscopy at 3.28 Å resolution. Released 18 Apr 2018.
Explore 5Z96 in 3D Show helices and sheets RCSB PDB PDBe
5Z96 contains 136 α-helices and 8 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 | 17-19 | 3 | 1 |
| α-helix | 31-39 | 9 | |
| α-helix | 45-53 | 9 | |
| α-helix | 76-79 | 4 | |
| α-helix | 83-91 | 9 | |
| α-helix | 99-105 | 7 | |
| α-helix | 111-116 | 6 | |
| α-helix | 145-151 | 7 | |
| α-helix | 155-162 | 8 | |
| β-strand | 167-169 | 3 | 2 |
| α-helix | 190-203 | 14 | |
| α-helix | 216-231 | 16 | |
| α-helix | 238-257 | 20 | |
| α-helix | 264-268 | 5 | |
| α-helix | 287-294 | 8 | |
| α-helix | 305-314 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 326-338 | 13 | |
| α-helix | 340-345 | 6 | |
| α-helix | 362-383 | 22 | |
| α-helix | 401-422 | 22 | |
| α-helix | 427-431 | 5 | |
| α-helix | 433-456 | 24 | |
| α-helix | 473-489 | 17 | |
| α-helix | 491-498 | 8 | |
| α-helix | 503-517 | 15 | |
| α-helix | 520-541 | 22 | |
| α-helix | 564-573 | 10 | |
| α-helix | 581-584 | 4 | |
| α-helix | 591-606 | 16 | |
| α-helix | 607-612 | 6 | |
| α-helix | 613-627 | 15 | |
| α-helix | 635-644 | 10 | |
| α-helix | 655-657 | 3 | |
| α-helix | 693-724 | 32 | |
| α-helix | 733-754 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Short transient receptor potential channel 4 | A, B, C, D | protein | 755 | Mus musculus | Q9QUQ5 (AlphaFold model) |
>5Z96_1 Short transient receptor potential channel 4 (chains A, B, C, D) MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFK ININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKK PSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVE CVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSE YEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEF VAQPNCQQLLASRWYDEFPGWRRRHWAVKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIR KPFIKFICHTASYLTFLFLLLLASQHIDRSDLNRQGPPPTIVEWMILPWVLGFIWGEIKQ MWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSALNPRESWDMWHPTLVAEAL FAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFY YEETKGLSCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATM FGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLPTPFNVI PSPKSLWYLVKWIWTHLCKKKMRRKPESFGTIGRRAADNLRRHHQYQEVMRNLVKRYVAA MIREAKTEEGLTEENVKELKQDISSFRFEVLGLLR
| ID | Name | Formula | Copies |
|---|---|---|---|
| LPP | 2-(hexadecanoyloxy)-1-[(phosphonooxy)methyl]ethyl hexadecanoate | C35 H69 O8 P | 4 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 4 |
Water and common crystallization additives (NA) are not listed.
Structure of the mouse TRPC4 ion channel. Duan, J., Li, J., Zeng, B. et al. Nat Commun (2018) 9:3102-3102. DOI 10.1038/s41467-018-05247-9 · PubMed
Other PDB entries of the same protein (UniProt Q9QUQ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5Z96 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.