the crystal structure of apo CASK-CaMK. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Aug 2025.
Explore 8Y68 in 3D Show helices and sheets RCSB PDB PDBe
8Y68 contains 39 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 |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| β-strand | 12-20 | 9 | 1 |
| β-strand | 24-31 | 8 | 1 |
| β-strand | 37-44 | 8 | 1 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 2 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 86-92 | 7 | 1 |
| β-strand | 98 | 1 | 2 |
| α-helix | 99-108 | 10 | |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 3 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 2 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 2 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-168 | 2 | 3 |
| β-strand | 175 | 1 | 4 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 4 |
| α-helix | 198-213 | 16 | |
| α-helix | 223-232 | 10 | |
| α-helix | 239-242 | 4 | |
| α-helix | 247-256 | 10 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-277 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-302 | 14 | |
| α-helix | 316-320 | 5 | |
| α-helix | 323-325 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-11 | 4 | |
| β-strand | 12-20 | 9 | 5 |
| β-strand | 24-31 | 8 | 5 |
| β-strand | 37-44 | 8 | 5 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 6 |
| β-strand | 77-83 | 7 | 5 |
| β-strand | 86-92 | 7 | 5 |
| β-strand | 98 | 1 | 6 |
| α-helix | 99-108 | 10 | |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 7 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 6 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 6 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-168 | 2 | 7 |
| β-strand | 175 | 1 | 8 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 8 |
| α-helix | 199-214 | 16 | |
| α-helix | 223-232 | 10 | |
| α-helix | 239-242 | 4 | |
| α-helix | 247-256 | 10 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-277 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-303 | 15 | |
| α-helix | 316-320 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peripheral plasma membrane protein CASK | A, B | protein | 338 | Homo sapiens | O14936 (AlphaFold model) |
>8Y68_1 Peripheral plasma membrane protein CASK (chains A, B) GPGSEFMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGL STEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYS EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGL VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK YKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQ LRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFS
Structural basis for the Ca 2+ /CaM-mediated regulation of CASK-CaMK. Li, W., Wang, Y., Feng, W. Int J Biol Macromol (2025) 332:148495-148495. DOI 10.1016/j.ijbiomac.2025.148495 · PubMed
Other PDB entries of the same protein (UniProt O14936 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8Y68 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.