Explore the Potential with AI-Driven Innovation
The specialised, focused library is developed on demand with the most recent virtual screening and parameter assessment technology, guided by the Receptor.AI drug discovery platform. This approach exceeds the capabilities of traditional methods and offers compounds with higher activity, selectivity, and safety.
The compounds are cherry-picked from the vast virtual chemical space of over 60B molecules. The synthesis and delivery of compounds is facilitated by our partner Reaxense.
The library features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
We utilise our cutting-edge, exclusive workflow to develop focused 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.
Key features that set our library apart include:
partner
Reaxense
upacc
Q15386
UPID:
UBE3C_HUMAN
Alternative names:
HECT-type ubiquitin transferase E3C; Homologous to E6AP carboxyl terminus homologous protein 2; RTA-associated ubiquitin ligase
Alternative UPACC:
Q15386; A4D235; A6NCP3; Q8TC15; Q96CR4; Q9UDU3
Background:
Ubiquitin-protein ligase E3C, known for its roles in protein ubiquitination, catalyzes 'Lys-29'- and 'Lys-48'-linked polyubiquitin chains. It interacts with the proteasome to promote ubiquitin chain elongation on substrates, facilitating their degradation. This protein also regulates autophagy and type I interferon response through targeted ubiquitination, showcasing its pivotal role in cellular processes.
Therapeutic significance:
Understanding the role of Ubiquitin-protein ligase E3C could open doors to potential therapeutic strategies.