Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced 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.
The library includes a list of the most effective modulators, each annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Furthermore, each compound is shown with its optimal docking poses, affinity scores, and activity scores, offering a detailed summary.
Our high-tech, dedicated method is applied to construct targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes comprehensive molecular simulations of the catalytic and allosteric binding pockets and the ensemble virtual screening accounting for their conformational mobility. In the case of designing modulators, the structural changes induced by reaction intermediates are taken into account to leverage activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q5XPI4
UPID:
RN123_HUMAN
Alternative names:
Kip1 ubiquitination-promoting complex protein 1; RING finger protein 123
Alternative UPACC:
Q5XPI4; A1L4Q3; A6NLS5; Q5I022; Q6PFW4; Q71RH0; Q8IW18; Q9H0M8; Q9H5L8; Q9H9T2
Background:
E3 ubiquitin-protein ligase RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 and RING finger protein 123, is a pivotal enzyme in protein ubiquitination. It serves as the catalytic subunit of the KPC complex, facilitating the ubiquitination and subsequent proteasomal degradation of CDKN1B, crucial for cell cycle progression. Additionally, RNF123 plays a significant role in NF-kappa-B signaling by promoting the maturation of NFKB1, and it acts as an inhibitor of antiviral signaling mediated by RIGI and IFIH1.
Therapeutic significance:
Understanding the role of E3 ubiquitin-protein ligase RNF123 could open doors to potential therapeutic strategies.