Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved activity, selectivity, and safety.
We carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
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.
We use our state-of-the-art dedicated workflow for designing 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
Q70JA7
UPID:
CHSS3_HUMAN
Alternative names:
Carbohydrate synthase 2; Chondroitin glucuronyltransferase 3; Chondroitin synthase 2; Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II; N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 3; N-acetylgalactosaminyltransferase 3
Alternative UPACC:
Q70JA7; B2RP97; Q76L22; Q86Y52
Background:
Chondroitin sulfate synthase 3, known for its roles as Carbohydrate synthase 2 and Chondroitin glucuronyltransferase 3 among others, is pivotal in the biosynthesis of chondroitin sulfate. It exhibits beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity, crucial for transferring glucuronic acid and N-acetylgalactosamine to the chondroitin polymer, albeit at a reduced activity compared to CHSY1.
Therapeutic significance:
Understanding the role of Chondroitin sulfate synthase 3 could open doors to potential therapeutic strategies.