Crystal structure of human alpha-dystroglycan. Determined by X-ray diffraction at 1.8 Å resolution. Released 12 Jul 2017.
Explore 5LLK in 3D Show helices and sheets RCSB PDB PDBe
5LLK contains 13 α-helices and 12 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 70-73 | 4 | 1 |
| β-strand | 78-81 | 4 | 2 |
| α-helix | 84-87 | 4 | |
| β-strand | 93-98 | 6 | 1 |
| α-helix | 104-105 | 2 | |
| β-strand | 108-111 | 4 | 2 |
| β-strand | 116-119 | 4 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 127-138 | 12 | 1 |
| β-strand | 144-157 | 14 | 1 |
| α-helix | 158 | 1 | |
| α-helix | 159-161 | 3 | |
| α-helix | 182-183 | 2 | |
| α-helix | 186-187 | 2 | |
| β-strand | 188-195 | 8 | 3 |
| α-helix | 199-201 | 3 | |
| α-helix | 204-218 | 15 | |
| α-helix | 222-224 | 3 | |
| β-strand | 225-229 | 5 | 3 |
| β-strand | 242-245 | 4 | 3 |
| β-strand | 256-264 | 9 | 3 |
| α-helix | 272-273 | 2 | |
| α-helix | 275-283 | 9 | |
| α-helix | 285-290 | 6 | |
| β-strand | 294-302 | 9 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dystroglycan | A | protein | 266 | Homo sapiens | Q14118 (AlphaFold model) |
>5LLK_1 Dystroglycan (chains A) GSSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLH WDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVHT ASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVP VVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQ LGYPVVGWHIANKKPPLPKRVRRQIH
Structural flexibility of human alpha-dystroglycan. Covaceuszach, S., Bozzi, M., Bigotti, M.G. et al. FEBS Open Bio (2017) 7:1064-1077. DOI 10.1002/2211-5463.12259 · PubMed
Other PDB entries of the same protein (UniProt Q14118 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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