Human Casein kinase 1 delta in complex with phosphorylated human PERIOD2 FASP peptide. Determined by X-ray diffraction at 1.65 Å resolution. Released 17 May 2023.
Explore 8D7O in 3D Show helices and sheets RCSB PDB PDBe
8D7O contains 35 α-helices and 30 β-strands across 4 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 | 4-5 | 2 | 1 |
| β-strand | 9-18 | 10 | 1 |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 34-41 | 8 | 1 |
| α-helix | 49-59 | 11 | |
| α-helix | 66-67 | 2 | |
| β-strand | 68-74 | 7 | 1 |
| β-strand | 77-83 | 7 | 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 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 4 |
| α-helix | 165-167 | 3 | |
| α-helix | 171-173 | 3 | |
| β-strand | 175 | 1 | 5 |
| α-helix | 182-185 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 192-208 | 17 | |
| α-helix | 221-234 | 14 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-257 | 12 | |
| α-helix | 262-264 | 3 | |
| α-helix | 266-279 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 6 |
| β-strand | 9-18 | 10 | 6 |
| β-strand | 21-28 | 8 | 6 |
| β-strand | 34-41 | 8 | 6 |
| α-helix | 49-59 | 11 | |
| α-helix | 66-67 | 2 | |
| β-strand | 68-74 | 7 | 6 |
| β-strand | 77-83 | 7 | 6 |
| β-strand | 88 | 1 | 7 |
| α-helix | 89-95 | 7 | |
| α-helix | 102-121 | 20 | |
| β-strand | 124-125 | 2 | 8 |
| α-helix | 131-133 | 3 | |
| β-strand | 134-136 | 3 | 7 |
| α-helix | 139-141 | 3 | |
| α-helix | 144 | 1 | |
| β-strand | 145-147 | 3 | 7 |
| β-strand | 154-155 | 2 | 8 |
| β-strand | 157 | 1 | 9 |
| α-helix | 163 | 1 | |
| β-strand | 164 | 1 | 9 |
| α-helix | 165-167 | 3 | |
| α-helix | 171-173 | 3 | |
| β-strand | 175 | 1 | 10 |
| α-helix | 182-185 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 192-208 | 17 | |
| α-helix | 221-234 | 14 | |
| α-helix | 237-240 | 4 | |
| α-helix | 246-257 | 12 | |
| α-helix | 262-264 | 3 | |
| α-helix | 266-280 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 666 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Casein kinase I isoform delta | A, B | protein | 301 | Homo sapiens | P48730 (AlphaFold model) |
| Period circadian protein homolog 2 peptide | C, D | protein | 16 | Homo sapiens | O15055 (AlphaFold model) |
>8D7O_1 Casein kinase I isoform delta (chains A, B) GAMDPEFMELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIES KIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMI SRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNL TGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKM STPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNML K
>8D7O_2 Period circadian protein homolog 2 peptide (chains C, D) GKAESVASLTSQCSYA
PERIOD phosphorylation leads to feedback inhibition of CK1 activity to control circadian period. Philpott, J.M., Freeberg, A.M., Park, J. et al. Mol Cell (2023) 83:1677-1692.e8. DOI 10.1016/j.molcel.2023.04.019 · 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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