Human Casein Kinase 1 delta Tau mutant (R178C). Determined by X-ray diffraction at 1.55 Å resolution. Released 12 Feb 2020.
Explore 6PXN in 3D Show helices and sheets RCSB PDB PDBe
6PXN contains 34 α-helices and 28 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 | 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 | |
| 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 | 139-143 | 5 | |
| α-helix | 144 | 1 | |
| 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 | |
| β-strand | 169 | 1 | 5 |
| α-helix | 182-185 | 4 | |
| β-strand | 188 | 1 | 5 |
| α-helix | 189-190 | 2 | |
| α-helix | 192-208 | 17 | |
| α-helix | 222-233 | 12 | |
| 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 | 49-58 | 10 | |
| 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 | |
| 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 | |
| α-helix | 289-292 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Casein kinase I isoform delta | A, B | protein | 415 | Homo sapiens | P48730 (AlphaFold model) |
>6PXN_1 Casein kinase I isoform delta (chains A, B) MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQ GGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIH SKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTACYA SINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL CKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRA ADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPV SGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
Casein kinase 1 dynamics underlie substrate selectivity and the PER2 circadian phosphoswitch. Philpott, J.M., Narasimamurthy, R., Ricci, C.G. et al. Elife (2020) 9. DOI 10.7554/eLife.52343 · 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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