EC Number   |
Inhibitors |
Structure |
|---|
   2.3.2.23 | more |
identification of an allosteric pocket on Ube2T through a fragment screening using biophysical methods. Several fragments binding to this site inhibit ubiquitin conjugation in vitro. One-dimensional 1H NMR spectroscopy, binding site identification through protein-observed NMR spectroscopy, and X-ray crystallography, overview. No inhibition by 5-(pyridin-2-yl)thiophene-2-carboxamide (EM29) |
 |
| 2.3.2.23 | more |
identification of ubiquitin variants that bind tightly and specifically to Ube2k at a hydrophobic cleft that is distinct from the active site and ubiquitin binding sites. The variants are potent inhibitors of Ube2k and block both ubiquitin charging of the E2 enzyme and E3-catalyzed ubiquitin transfer |
|
| 2.3.2.23 | more |
generation of ubiquitin variants that inhibit the E2 enzyme. The variants inhibit ubiquitin chain building, and bind to UB2D2 with low micromolar affinity and high specificity. The binding site overlaps with E1 binding, and the variants can have an additional binding site that blocks a critical non-covalent ubiquitin-binding site on the E2 enzyme |
|
| 2.3.2.23 | [1,1'-biphenyl]-2,2'-diol |
- |
  |
| 2.3.2.23 | [1,1'-biphenyl]-2-ol |
- |
|
| 2.3.2.23 | [1,1'-biphenyl]-2-sulfonamide |
- |
|
