14-3-3 epsilon bound to phosphorylated PEAK2 (pS826) peptide. Determined by X-ray diffraction at 3.16 Å resolution. Released 7 Jun 2023.
Explore 8DGN in 3D Show helices and sheets RCSB PDB PDBe
8DGN contains 10 α-helices and 0 β-strands across 1 chain. 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 | 39-71 | 33 | |
| α-helix | 77-103 | 27 | |
| α-helix | 104-108 | 5 | |
| α-helix | 115-135 | 21 | |
| α-helix | 139-162 | 24 | |
| α-helix | 168-179 | 12 | |
| α-helix | 180-184 | 5 | |
| α-helix | 188-205 | 18 | |
| α-helix | 211-213 | 3 | |
| α-helix | 215-231 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein epsilon | A | protein | 258 | Homo sapiens | P62258 (AlphaFold model) |
| Phosphorylated PEAK2 (pS826) peptide | B | protein | 20 | Homo sapiens | Q86YV5 (AlphaFold model) |
>8DGN_1 14-3-3 protein epsilon (chains A) GSTMDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARR ASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGES KVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNF SVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQG DGEEQNKEALQDVEDENQ
>8DGN_2 Phosphorylated PEAK2 (pS826) peptide (chains B) PPPLPQKKIVSRAASSPDGF
Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling. Roy, M.J., Surudoi, M.G., Kropp, A. et al. Nat Commun (2023) 14:3542-3542. DOI 10.1038/s41467-023-38869-9 · PubMed
Other PDB entries of the same protein (UniProt P62258 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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