Structure of the PEAK3 pseudokinase homodimer. Determined by electron microscopy at 4.9 Å resolution. Released 28 Jun 2023.
Explore 8DS6 in 3D Show helices and sheets RCSB PDB PDBe
8DS6 contains 41 α-helices and 25 β-strands across 2 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 | 131-157 | 27 | |
| α-helix | 161-165 | 5 | |
| α-helix | 169 | 1 | |
| β-strand | 170-173 | 4 | 1 |
| β-strand | 180-181 | 2 | 1 |
| β-strand | 185-194 | 10 | 1 |
| β-strand | 197-206 | 10 | 1 |
| α-helix | 207 | 1 | |
| α-helix | 216-221 | 6 | |
| α-helix | 225-226 | 2 | |
| β-strand | 230 | 1 | 2 |
| β-strand | 233-237 | 5 | 1 |
| β-strand | 251-254 | 4 | 1 |
| β-strand | 260-261 | 2 | 2 |
| α-helix | 262-269 | 8 | |
| α-helix | 274-298 | 25 | |
| β-strand | 300-302 | 3 | 3 |
| α-helix | 307-309 | 3 | |
| β-strand | 310-313 | 4 | 2 |
| α-helix | 314-315 | 2 | |
| α-helix | 323-324 | 2 | |
| β-strand | 325-328 | 4 | 2 |
| α-helix | 331-333 | 3 | |
| β-strand | 334-336 | 3 | 3 |
| α-helix | 344-346 | 3 | |
| α-helix | 349-360 | 12 | |
| α-helix | 364-365 | 2 | |
| α-helix | 369-383 | 15 | |
| α-helix | 388-399 | 12 | |
| α-helix | 420-439 | 20 | |
| α-helix | 443-446 | 4 | |
| α-helix | 447-458 | 12 | |
| α-helix | 461-472 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 131-157 | 27 | |
| α-helix | 162-165 | 4 | |
| β-strand | 169-173 | 5 | 4 |
| β-strand | 180-182 | 3 | 4 |
| β-strand | 185-194 | 10 | 4 |
| β-strand | 197-206 | 10 | 4 |
| α-helix | 207 | 1 | |
| α-helix | 215-223 | 9 | |
| α-helix | 225-226 | 2 | |
| β-strand | 230 | 1 | 5 |
| β-strand | 233-237 | 5 | 4 |
| β-strand | 251-254 | 4 | 4 |
| β-strand | 260-261 | 2 | 6 |
| α-helix | 262-269 | 8 | |
| α-helix | 278-297 | 20 | |
| β-strand | 300-302 | 3 | 7 |
| α-helix | 307-309 | 3 | |
| β-strand | 311-313 | 3 | 6 |
| α-helix | 314-315 | 2 | |
| α-helix | 323-324 | 2 | |
| β-strand | 325-327 | 3 | 6 |
| β-strand | 328 | 1 | 5 |
| α-helix | 331-333 | 3 | |
| β-strand | 334-336 | 3 | 7 |
| α-helix | 349-362 | 14 | |
| α-helix | 365 | 1 | |
| α-helix | 369-384 | 16 | |
| α-helix | 388-399 | 12 | |
| α-helix | 416-419 | 4 | |
| α-helix | 420-440 | 21 | |
| α-helix | 443-446 | 4 | |
| α-helix | 447-458 | 12 | |
| α-helix | 461-471 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein PEAK3 | A, B | protein | 491 | Homo sapiens | Q6ZS72 (AlphaFold model) |
>8DS6_1 Protein PEAK3 (chains A, B) MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLP KKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAP LGLSLRDLHSPEAVHTALAARQLQGLRTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCA ESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEG TLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGA ALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALL SLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRAL GPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWDLEGGGGA DYKDDDDKGPV
Structural insights into regulation of the PEAK3 pseudokinase scaffold by 14-3-3. Torosyan, H., Paul, M.D., Forget, A. et al. Nat Commun (2023) 14:3543-3543. DOI 10.1038/s41467-023-38864-0 · PubMed
Other PDB entries of the same protein (UniProt Q6ZS72 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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