the crystal structure of the Ca2+/CaM-CASK-CaMK complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Nov 2025.
Explore 9M5Y in 3D Show helices and sheets RCSB PDB PDBe
9M5Y contains 23 α-helices and 15 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 | 97-98 | 2 | 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 |
| β-strand | 167-168 | 2 | 3 |
| β-strand | 174-175 | 2 | 4 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196-197 | 2 | 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 | 289-311 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 84-93 | 10 | |
| β-strand | 100-101 | 2 | 5 |
| α-helix | 103-112 | 10 | |
| α-helix | 116-118 | 3 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137-138 | 2 | 5 |
| α-helix | 139-146 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peripheral plasma membrane protein CASK | A | protein | 338 | Homo sapiens | O14936 (AlphaFold model) |
| Calmodulin-1 | B | protein | 153 | Rattus norvegicus | P0DP29 (AlphaFold model) |
>9M5Y_1 Peripheral plasma membrane protein CASK (chains A) GPGSEFMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGL STEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYS EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGL VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK YKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQ LRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFS
>9M5Y_2 Calmodulin-1 (chains B) GPGSMADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEV DADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEK LTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
| CA | Calcium ion | Ca | 2 |
| PO4 | Phosphate ion | O4 P | 1 |
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:
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