Crystal Structure of CK2alpha with a novel closed conformation of the aD loop. Determined by X-ray diffraction at 1.25 Å resolution. Released 27 Jul 2016.
Explore 5CVG in 3D Show helices and sheets RCSB PDB PDBe
5CVG contains 22 α-helices and 11 β-strands across 1 chain. 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 | 21-24 | 4 | |
| α-helix | 26-28 | 3 | |
| α-helix | 36-38 | 3 | |
| β-strand | 39-47 | 9 | 1 |
| β-strand | 51-58 | 8 | 1 |
| β-strand | 63-70 | 8 | 1 |
| α-helix | 71 | 1 | |
| α-helix | 75-88 | 14 | |
| β-strand | 94 | 1 | 2 |
| β-strand | 96-102 | 7 | 1 |
| β-strand | 109-114 | 6 | 1 |
| β-strand | 122-123 | 2 | 2 |
| α-helix | 130-149 | 20 | |
| β-strand | 152-153 | 2 | 3 |
| α-helix | 159-161 | 3 | |
| β-strand | 162-165 | 4 | 2 |
| β-strand | 170-173 | 4 | 2 |
| α-helix | 176-178 | 3 | |
| β-strand | 180-181 | 2 | 3 |
| α-helix | 195-197 | 3 | |
| α-helix | 200-203 | 4 | |
| α-helix | 212-227 | 16 | |
| α-helix | 238-249 | 12 | |
| α-helix | 251-261 | 11 | |
| α-helix | 267-272 | 6 | |
| α-helix | 277-280 | 4 | |
| α-helix | 281-284 | 4 | |
| α-helix | 290-292 | 3 | |
| α-helix | 295-304 | 10 | |
| α-helix | 309-311 | 3 | |
| α-helix | 313-314 | 2 | |
| α-helix | 315-319 | 5 | |
| α-helix | 322-324 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Casein kinase II subunit alpha | A | protein | 351 | Homo sapiens | P68400 (AlphaFold model) |
>5CVG_1 Casein kinase II subunit alpha (chains A) GSMDIEFDDDADDDGSGSGSGSGSGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDD YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLA DIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVK PHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSL GCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSR KRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVK
Specific inhibition of CK2 alpha from an anchor outside the active site. Brear, P., De Fusco, C., Hadje Georgiou, K. et al. Chem Sci (2016) 7:6839-6845. DOI 10.1039/c6sc02335e · PubMed
Other PDB entries of the same protein (UniProt P68400 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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