6LNM: CASK-CaMK
Crystal structure of CASK-CaMK in complex with Mint1-CID. Determined by X-ray diffraction at 2.4 Å resolution. Released 8 Apr 2020.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organisms
- Rattus norvegicus, Mus musculus
- Chains
- 6
- Atoms
- 8,985
- Mol. weight
- 135.72 kDa
- Released
- 8 Apr 2020
Explore 6LNM in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6LNM contains 73 α-helices and 47 β-strands across 6 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.
Chain A: 22 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| β-strand | 12-20 | 9 | 1 |
| β-strand | 25-31 | 7 | 1 |
| β-strand | 37-44 | 8 | 1 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 69-70 | 2 | 2 |
| β-strand | 74 | 1 | 3 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 86-92 | 7 | 1 |
| α-helix | 93 | 1 | |
| β-strand | 98 | 1 | 3 |
| α-helix | 99-108 | 10 | |
| β-strand | 111 | 1 | 4 |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 5 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 3 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 3 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-168 | 2 | 5 |
| β-strand | 175 | 1 | 6 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 6 |
| 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 | 289-302 | 14 | |
| α-helix | 316-320 | 5 | |
| α-helix | 323-328 | 6 | |
Chain B: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 348-351 | 4 | |
| α-helix | 352-367 | 16 | |
| β-strand | 370-371 | 2 | 2 |
| α-helix | 375-379 | 5 | |
| β-strand | 386 | 1 | 4 |
Chain C: 22 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| β-strand | 12-20 | 9 | 7 |
| β-strand | 25-31 | 7 | 7 |
| β-strand | 37-44 | 8 | 7 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 8 |
| β-strand | 77-83 | 7 | 7 |
| β-strand | 86-92 | 7 | 7 |
| α-helix | 93 | 1 | |
| β-strand | 98 | 1 | 8 |
| α-helix | 99-108 | 10 | |
| β-strand | 111 | 1 | 9 |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 10 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 8 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 8 |
| α-helix | 163-165 | 3 | |
| β-strand | 167-168 | 2 | 10 |
| β-strand | 175 | 1 | 11 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 11 |
| 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 | 289-302 | 14 | |
| α-helix | 316-320 | 5 | |
| α-helix | 323-328 | 6 | |
Chain D: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 348-351 | 4 | |
| α-helix | 352-368 | 17 | |
| β-strand | 386 | 1 | 9 |
Chain E: 21 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-11 | 4 | |
| β-strand | 12-20 | 9 | 12 |
| β-strand | 25-31 | 7 | 12 |
| β-strand | 37-44 | 8 | 12 |
| α-helix | 45-49 | 5 | |
| α-helix | 56-68 | 13 | |
| β-strand | 74 | 1 | 13 |
| β-strand | 77-83 | 7 | 12 |
| β-strand | 86-92 | 7 | 12 |
| α-helix | 93 | 1 | |
| β-strand | 98 | 1 | 13 |
| α-helix | 99-108 | 10 | |
| β-strand | 111 | 1 | 14 |
| α-helix | 115-134 | 20 | |
| β-strand | 137-138 | 2 | 15 |
| α-helix | 144-146 | 3 | |
| β-strand | 147-149 | 3 | 13 |
| α-helix | 156-157 | 2 | |
| β-strand | 158-160 | 3 | 13 |
| β-strand | 167-168 | 2 | 15 |
| β-strand | 175 | 1 | 16 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-191 | 4 | |
| β-strand | 196 | 1 | 16 |
| 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 | 289-302 | 14 | |
| α-helix | 316-320 | 5 | |
| α-helix | 323-329 | 7 | |
Chain F: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 348-351 | 4 | |
| α-helix | 352-367 | 16 | |
| α-helix | 375-378 | 4 | |
| β-strand | 386 | 1 | 14 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Peripheral plasma membrane protein CASK | A, C, E | protein | 351 | Rattus norvegicus | Q62915 (AlphaFold model) |
| Amyloid-beta A4 precursor protein-binding family A member 1 | B, D, F | protein | 50 | Mus musculus | B2RUJ5 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>6LNM_1 Peripheral plasma membrane protein CASK (chains A, C, E)
GPGSEFMADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGL
STEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYS
EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGL
VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK
YKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQ
LRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAER
Sequence of entity 2 (B, D, F), FASTA
>6LNM_2 Amyloid-beta A4 precursor protein-binding family A member 1 (chains B, D, F)
GPGSEFISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTR
Primary citation
Structural Basis for the High-Affinity Interaction between CASK and Mint1. Wu, X., Cai, Q., Chen, Y. et al. Structure (2020) 28:664-673.e3. DOI 10.1016/j.str.2020.04.001 · PubMed
Other PDB entries of the same protein (UniProt Q62915 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1RSO Hetero-tetrameric L27 (Lin-2, Lin-7) domain complexes as organization platforms of…
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