Structural basis for the recognition of Lys48-linked polyubiquitin chain by the Josephin domain of ataxin-3, a putative deubiquitinating enzyme. Determined by solution NMR. Released 22 May 2007.
Explore 2DOS in 3D Show helices and sheets RCSB PDB PDBe
2DOS contains 6 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 15-22 | 8 | |
| α-helix | 30-49 | 20 | |
| α-helix | 55-62 | 8 | |
| α-helix | 77-85 | 9 | |
| β-strand | 90-93 | 4 | 1 |
| α-helix | 97-102 | 6 | |
| β-strand | 111-116 | 6 | 1 |
| β-strand | 119-126 | 8 | 1 |
| β-strand | 129-133 | 5 | 1 |
| β-strand | 141-143 | 3 | 1 |
| α-helix | 145-158 | 14 | |
| β-strand | 161-166 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ataxin-3 | A | protein | 176 | Homo sapiens | P54252 (AlphaFold model) |
>2DOS_1 Ataxin-3 (chains A) GPLGSMESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTS EDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICN YKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPD
Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinase activity. Satoh, T., Sumiyoshi, A., Yagi-Utsumi, M. et al. FEBS Lett (2014) 588:4422-4430. DOI 10.1016/j.febslet.2014.10.013 · PubMed
Other PDB entries of the same protein (UniProt P54252 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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