Crystal structure of an OTU deubiquitinase from Escherichia albertii bound to ubiquitin. Determined by X-ray diffraction at 2.1 Å resolution. Released 1 Jul 2020.
Explore 6W9S in 3D Show helices and sheets RCSB PDB PDBe
6W9S contains 13 α-helices and 11 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 | 196-209 | 14 | |
| α-helix | 217-232 | 16 | |
| β-strand | 237-241 | 5 | 1 |
| β-strand | 254-258 | 5 | 1 |
| β-strand | 263-267 | 5 | 1 |
| β-strand | 275-277 | 3 | 1 |
| α-helix | 278 | 1 | |
| α-helix | 285-297 | 13 | |
| α-helix | 306-308 | 3 | |
| α-helix | 313-327 | 15 | |
| α-helix | 329-332 | 4 | |
| α-helix | 333-343 | 11 | |
| α-helix | 346-358 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-7 | 7 | 2 |
| β-strand | 12-17 | 6 | 2 |
| β-strand | 22 | 1 | 3 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 2 |
| β-strand | 48-49 | 2 | 2 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 3 |
| α-helix | 56-59 | 4 | |
| β-strand | 66-70 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| OTU domain-containing protein EschOTU | A | protein | 179 | Escherichia albertii (strain TW07627) | B1EF49 |
| Ubiquitin | B | protein | 78 | Homo sapiens | F5H388 (AlphaFold model) |
>6W9S_1 OTU domain-containing protein EschOTU (chains A) SSPQSVFSDSVSSSRLELKKQIIKALDLDYWQGSGGEIMPLVLIDFYKRHNININIYLNH CKVNNFDKKAINLINAGNHYNALTMNSRGNIERIDVPGDGNCLYHAVVKSHQITRKPKPY GNELQKDKPEWCILKESLKTHFDKDFDQFVEQVKCILISENTHEANKILDKVAQYSGVK
>6W9S_2 Ubiquitin (chains B) GPMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSD YNIQKESTLHLVLRLRGX
Identification and characterization of diverse OTU deubiquitinases in bacteria. Schubert, A.F., Nguyen, J.V., Franklin, T.G. et al. EMBO J (2020) 39:e105127-e105127. DOI 10.15252/embj.2020105127 · PubMed
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