CASK CaM-Kinase Domain- AMPPNP complex, P1 form. Determined by X-ray diffraction at 2.3 Å resolution. Released 29 Apr 2008.
Explore 3C0H in 3D Show helices and sheets RCSB PDB PDBe
3C0H contains 38 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 | 8-11 | 4 | |
| 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 | 199-214 | 16 | |
| α-helix | 223-232 | 10 | |
| α-helix | 239-242 | 4 | |
| α-helix | 247-256 | 10 | |
| α-helix | 265-266 | 2 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-277 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-303 | 15 |
| 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 |
| α-helix | 75-76 | 2 | |
| 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 |
| 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 | 265-266 | 2 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-277 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 289-303 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peripheral plasma membrane protein CASK | A, B | protein | 351 | Homo sapiens | O14936 (AlphaFold model) |
>3C0H_1 Peripheral plasma membrane protein CASK (chains A, B) GSPGISGGGGGILDMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVA KFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKR ADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVA IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERL FEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKI HLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTS
| ID | Name | Formula | Copies |
|---|---|---|---|
| AMP | Adenosine monophosphate | C10 H14 N5 O7 P | 2 |
CASK Functions as a Mg2+-independent neurexin kinase. Mukherjee, K., Sharma, M., Urlaub, H. et al. Cell (2008) 133:328-339. DOI 10.1016/j.cell.2008.02.036 · PubMed
Other PDB entries of the same protein (UniProt O14936 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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