Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior activity, selectivity and safety.
We pick out particular compounds from an extensive virtual database of more than 60 billion molecules. The preparation and shipment of these compounds are facilitated by our associate Reaxense.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
Our high-tech, dedicated method is applied to construct targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The procedure entails thorough molecular simulations of the catalytic and allosteric binding pockets, accompanied by ensemble virtual screening that factors in their conformational flexibility. When developing modulators, the structural modifications brought about by reaction intermediates are factored in to optimize activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
O00762
UPID:
UBE2C_HUMAN
Alternative names:
(E3-independent) E2 ubiquitin-conjugating enzyme C; E2 ubiquitin-conjugating enzyme C; UbcH10; Ubiquitin carrier protein C; Ubiquitin-protein ligase C
Alternative UPACC:
O00762; A6NP33; E1P5N7; G3XAB7
Background:
Ubiquitin-conjugating enzyme E2 C (UbcH10), also known as Ubiquitin carrier protein C, plays a pivotal role in cell cycle regulation. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins, facilitating 'Lys-11'- and 'Lys-48'-linked polyubiquitination. This enzyme is a crucial component of the anaphase promoting complex/cyclosome (APC/C), which is essential for mitotic exit by degrading APC/C substrates via the proteasome.
Therapeutic significance:
Understanding the role of Ubiquitin-conjugating enzyme E2 C could open doors to potential therapeutic strategies.