7A6Y: 14-3-3 gamma
Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A. Determined by X-ray diffraction at 2.5 Å resolution. Released 25 Aug 2021.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 7,579
- Mol. weight
- 114.57 kDa
- Ligands
- FSC
- Released
- 25 Aug 2021
Explore 7A6Y in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7A6Y contains 54 α-helices and 0 β-strands across 7 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.
Chain A: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-32 | 13 | |
| α-helix | 39-69 | 31 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 117-137 | 21 | |
| α-helix | 140-142 | 3 | |
| α-helix | 143-164 | 22 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 217-233 | 17 | |
Chain B: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-32 | 13 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-67 | 29 | |
| α-helix | 80-103 | 24 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-135 | 19 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-205 | 16 | |
| α-helix | 219-232 | 14 | |
Chain C: 13 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-32 | 13 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-73 | 35 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 117-137 | 21 | |
| α-helix | 140-164 | 25 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-207 | 18 | |
| α-helix | 217-232 | 16 | |
Chain D: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-16 | 12 | |
| α-helix | 20-32 | 13 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-71 | 33 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-137 | 21 | |
| α-helix | 143-164 | 22 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 216-233 | 18 | |
Chains J and L: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 366-368 | 3 | |
Chain K: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 365-368 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 14-3-3 protein gamma | A, B, C, D | protein | 236 | Homo sapiens | P61981 (AlphaFold model) |
| DAPK2 C-terminal peptide | J, K, L, M | protein | 7 | Homo sapiens | Q9UIK4 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>7A6Y_1 14-3-3 protein gamma (chains A, B, C, D)
GHMVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRS
SWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYE
SKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALN
YSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWT
Sequence of entity 2 (J, K, L, M), FASTA
>7A6Y_2 DAPK2 C-terminal peptide (chains J, K, L, M)
RRRSSTS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| FSC | Fusicoccin | C36 H56 O12 | 3 |
Primary citation
14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites. Horvath, M., Petrvalska, O., Herman, P. et al. Commun Biol (2021) 4:986-986. DOI 10.1038/s42003-021-02518-y · PubMed
Other PDB entries of the same protein (UniProt P61981 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6S9K 1.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding…
- 6ZBT 1.8 Å, Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser342
- 3UZD 1.86 Å, Crystal structure of 14-3-3 GAMMA
- 6ZC9 1.9 Å, Structure of 14-3-3 gamma in complex with Nedd4-2 14-3-3 binding motif Ser448
- 6A5S 2.1 Å, Structure of 14-3-3 gamma in complex with TFEB 14-3-3 binding motif
- 4E2E 2.25 Å, Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation…
- 2B05 2.55 Å, Crystal Structure of 14-3-3 gamma in complex with a phosphoserine peptide
- 6GKF 2.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 14-3-3 binding motif Ser139
- 6BZD 2.67 Å, Structure of 14-3-3 gamma R57E mutant bound to GlcNAcylated peptide
- 7A6R 2.7 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide containing the 14-3-3 binding…
- 5D3E 2.75 Å, Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795
- 6SAD 2.75 Å, Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on…
Browse structure collections
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