Structure of the PEAK3/14-3-3 complex. Determined by electron microscopy at 3.1 Å resolution. Released 28 Jun 2023.
Explore 8DP5 in 3D Show helices and sheets RCSB PDB PDBe
8DP5 contains 67 α-helices and 25 β-strands across 5 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 | |
| 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 | 215-221 | 7 | |
| α-helix | 225-226 | 2 | |
| β-strand | 230 | 1 | 2 |
| β-strand | 233-237 | 5 | 1 |
| α-helix | 238 | 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 | 345-346 | 2 | |
| α-helix | 349-360 | 12 | |
| α-helix | 364-365 | 2 | |
| α-helix | 369-384 | 16 | |
| α-helix | 388-399 | 12 | |
| α-helix | 420-441 | 22 | |
| α-helix | 443-446 | 4 | |
| α-helix | 447-456 | 10 | |
| α-helix | 461-472 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 131-157 | 27 | |
| α-helix | 161-165 | 5 | |
| β-strand | 170-173 | 4 | 4 |
| β-strand | 180-181 | 2 | 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 | 277-297 | 21 | |
| β-strand | 300-302 | 3 | 7 |
| 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 | 364-365 | 2 | |
| α-helix | 369-384 | 16 | |
| α-helix | 388-399 | 12 | |
| α-helix | 420-440 | 21 | |
| α-helix | 443-446 | 4 | |
| α-helix | 447-457 | 11 | |
| α-helix | 461-471 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 21-32 | 12 | |
| α-helix | 36-39 | 4 | |
| α-helix | 40-70 | 31 | |
| α-helix | 75-102 | 28 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-132 | 19 | |
| α-helix | 138-161 | 24 | |
| α-helix | 167-182 | 16 | |
| α-helix | 187-202 | 16 | |
| α-helix | 205-207 | 3 | |
| α-helix | 210-231 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-70 | 32 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 115-135 | 21 | |
| α-helix | 139-162 | 24 | |
| α-helix | 168-180 | 13 | |
| α-helix | 181-185 | 5 | |
| α-helix | 188-203 | 16 | |
| α-helix | 206-208 | 3 | |
| α-helix | 211-232 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 69-71 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein PEAK3 | A, B | protein | 491 | Homo sapiens | Q6ZS72 (AlphaFold model) |
| 14-3-3 protein beta/alpha | C | protein | 246 | Homo sapiens | P31946 (AlphaFold model) |
| 14-3-3 protein epsilon | D | protein | 255 | Homo sapiens | P62258 (AlphaFold model) |
| Protein PEAK3 fragment | E, P | protein | 491 | Homo sapiens | Q6ZS72 (AlphaFold model) |
>8DP5_1 Protein PEAK3 (chains A, B) MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLP KKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAP LGLSLRDLHSPEAVHTALAARQLQGLRTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCA ESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEG TLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGA ALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALL SLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRAL GPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWDLEGGGGA DYKDDDDKGPV
>8DP5_2 14-3-3 protein beta/alpha (chains C) MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSS WRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFY LKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFY YEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGD AGEGEN
>8DP5_3 14-3-3 protein epsilon (chains D) MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASW RIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVF YYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVF YYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGE EQNKEALQDVEDENQ
>8DP5_4 Protein PEAK3 fragment (chains E, P) 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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