Structure of 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser511. Determined by X-ray diffraction at 2.84 Å resolution. Released 10 Jan 2018.
Explore 6FEL in 3D Show helices and sheets RCSB PDB PDBe
6FEL contains 49 α-helices and 0 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 | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 39-73 | 35 | |
| α-helix | 79-103 | 25 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 117-137 | 21 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-185 | 16 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 217-232 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 39-67 | 29 | |
| α-helix | 78-103 | 26 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-135 | 19 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-185 | 16 | |
| α-helix | 190-206 | 17 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-231 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 39-73 | 35 | |
| α-helix | 78-103 | 26 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-135 | 19 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-205 | 16 | |
| α-helix | 217-232 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-16 | 13 | |
| α-helix | 20-31 | 12 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-68 | 30 | |
| α-helix | 78-103 | 26 | |
| 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 | 190-205 | 16 | |
| α-helix | 208-210 | 3 | |
| α-helix | 216-233 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 509-513 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein gamma | A, B, C, D | protein | 236 | Homo sapiens | P61981 (AlphaFold model) |
| Calcium/calmodulin-dependent protein kinase kinase 2 | E, F, G, H | protein | 8 | Homo sapiens | Q96RR4 (AlphaFold model) |
>6FEL_1 14-3-3 protein gamma (chains A, B, C, D) GHMVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRS SWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYE SKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALN YSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWT
>6FEL_2 Calcium/calmodulin-dependent protein kinase kinase 2 (chains E, F, G, H) RSLSAPGN
14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2). Psenakova, K., Petrvalska, O., Kylarova, S. et al. Biochim Biophys Acta (2018) 1862:1612-1625. DOI 10.1016/j.bbagen.2018.04.006 · PubMed
Other PDB entries of the same protein (UniProt P61981 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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