Crystal structure of phosphorylated pT220 Casein Kinase I delta (CK1d), conformation 2 and 3. Determined by X-ray diffraction at 1.7 Å resolution. Released 13 Apr 2022.
Explore 7P7G in 3D Show helices and sheets RCSB PDB PDBe
7P7G contains 34 α-helices and 26 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 |
|---|---|---|---|
| β-strand | 9-18 | 10 | 1 |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 33-40 | 8 | 1 |
| α-helix | 49-58 | 10 | |
| β-strand | 68-74 | 7 | 1 |
| β-strand | 77-82 | 6 | 1 |
| β-strand | 88 | 1 | 2 |
| α-helix | 89-95 | 7 | |
| α-helix | 102-121 | 20 | |
| β-strand | 124-125 | 2 | 3 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-136 | 3 | 2 |
| α-helix | 139-141 | 3 | |
| β-strand | 145-147 | 3 | 2 |
| β-strand | 154-155 | 2 | 3 |
| β-strand | 157 | 1 | 4 |
| β-strand | 164 | 1 | 4 |
| α-helix | 165-167 | 3 | |
| α-helix | 171-173 | 3 | |
| α-helix | 182-185 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 192-208 | 17 | |
| α-helix | 218-219 | 2 | |
| α-helix | 226-233 | 8 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-257 | 11 | |
| α-helix | 262-264 | 3 | |
| α-helix | 266-279 | 14 | |
| α-helix | 289-292 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-17 | 9 | 5 |
| β-strand | 22-28 | 7 | 5 |
| β-strand | 33-41 | 9 | 5 |
| α-helix | 49-59 | 11 | |
| β-strand | 68-74 | 7 | 5 |
| β-strand | 77-83 | 7 | 5 |
| β-strand | 88 | 1 | 6 |
| α-helix | 89-95 | 7 | |
| α-helix | 102-121 | 20 | |
| β-strand | 124-125 | 2 | 7 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-136 | 3 | 6 |
| α-helix | 139-141 | 3 | |
| α-helix | 144 | 1 | |
| β-strand | 145-147 | 3 | 6 |
| β-strand | 154-155 | 2 | 7 |
| β-strand | 157 | 1 | 8 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 8 |
| α-helix | 165-166 | 2 | |
| β-strand | 169 | 1 | 9 |
| α-helix | 182-185 | 4 | |
| β-strand | 188 | 1 | 9 |
| α-helix | 189-190 | 2 | |
| α-helix | 192-208 | 17 | |
| α-helix | 221-233 | 13 | |
| α-helix | 237-240 | 4 | |
| α-helix | 247-257 | 11 | |
| α-helix | 262-264 | 3 | |
| α-helix | 266-280 | 15 | |
| α-helix | 289-291 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Casein kinase I isoform delta | A, B | protein | 296 | Homo sapiens | P48730 (AlphaFold model) |
>7P7G_1 Casein kinase I isoform delta (chains A, B) SMMELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKM MQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEY IHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTAR YASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIE VLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLK
Water and common crystallization additives (EDO) are not listed.
Kinase domain autophosphorylation rewires the activity and substrate specificity of CK1 enzymes. Cullati, S.N., Chaikuad, A., Chen, J.S. et al. Mol Cell (2022) 82:2006. DOI 10.1016/j.molcel.2022.03.005 · PubMed
Other PDB entries of the same protein (UniProt P48730 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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