The crystal structure of CASK/Mint1 complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 5 Aug 2020.
Explore 6KMH in 3D Show helices and sheets RCSB PDB PDBe
6KMH contains 51 α-helices and 30 β-strands across 4 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 | 12-21 | 10 | 1 |
| β-strand | 24-31 | 8 | 1 |
| β-strand | 37-44 | 8 | 1 |
| α-helix | 45-50 | 6 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 2 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 86-92 | 7 | 1 |
| α-helix | 93 | 1 | |
| β-strand | 98 | 1 | 2 |
| α-helix | 99-108 | 10 | |
| β-strand | 111 | 1 | 3 |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 4 |
| 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 | 4 |
| β-strand | 175 | 1 | 5 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 5 |
| 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 | 289-300 | 12 | |
| α-helix | 305-311 | 7 | |
| α-helix | 314-317 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-11 | 4 | |
| β-strand | 12-21 | 10 | 6 |
| β-strand | 24-31 | 8 | 6 |
| β-strand | 37-44 | 8 | 6 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 7 |
| β-strand | 77-83 | 7 | 6 |
| β-strand | 86-92 | 7 | 6 |
| α-helix | 93 | 1 | |
| β-strand | 98 | 1 | 7 |
| α-helix | 99-108 | 10 | |
| β-strand | 111 | 1 | 8 |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 9 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 7 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 7 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-168 | 2 | 9 |
| β-strand | 175 | 1 | 10 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 10 |
| 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 | 289-300 | 12 | |
| α-helix | 305-311 | 7 | |
| α-helix | 314-318 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 342-364 | 23 | |
| α-helix | 366-369 | 4 | |
| α-helix | 374-376 | 3 | |
| β-strand | 383 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -1-339 | 4 | |
| α-helix | 342-364 | 23 | |
| α-helix | 366-369 | 4 | |
| α-helix | 373-376 | 4 | |
| β-strand | 383 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peripheral plasma membrane protein CASK | A, B | protein | 325 | Homo sapiens | O14936 (AlphaFold model) |
| Amyloid-beta A4 precursor protein-binding family A member 1 | C, D | protein | 66 | Rattus norvegicus | O35430 (AlphaFold model) |
>6KMH_1 Peripheral plasma membrane protein CASK (chains A, B) GPGSEFMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGL STEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYS EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGL VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK YKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQ LRKFNARRKLKGAVLAAVSSHKFNS
>6KMH_2 Amyloid-beta A4 precursor protein-binding family A member 1 (chains C, D) GPGSEFQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTR DCDDQR
CASK modulates the assembly and function of the Mint1/Munc18-1 complex to regulate insulin secretion. Zhang, Z., Li, W., Yang, G. et al. Cell Discov (2020) 6:92-92. DOI 10.1038/s41421-020-00216-3 · 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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