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 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.
The library includes a list of the most promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
Our top-notch dedicated system is used to design specialised 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
Q9Y662
UPID:
HS3SB_HUMAN
Alternative names:
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1
Alternative UPACC:
Q9Y662; B3KN58; D3DTS6
Background:
Heparan sulfate glucosamine 3-O-sulfotransferase 3B1, also known as Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1, plays a crucial role in modifying heparan sulfate. This modification involves the transfer of a sulfo group to glucosamine, facilitating the creation of a specific heparan sulfate that serves as a receptor for Herpes simplex virus-1 (HSV-1) entry. This process does not affect the anticoagulant properties of heparan sulfate.
Therapeutic significance:
Understanding the role of Heparan sulfate glucosamine 3-O-sulfotransferase 3B1 could open doors to potential therapeutic strategies, particularly in preventing HSV-1 infection by targeting the enzyme's substrate-specific modifications.