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.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner 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.
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.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
P50226
UPID:
ST1A2_HUMAN
Alternative names:
Aryl sulfotransferase 2; Phenol sulfotransferase 2; Phenol-sulfating phenol sulfotransferase 2
Alternative UPACC:
P50226; A9QY25; P78393; Q14CJ7
Background:
Sulfotransferase 1A2, known alternatively as Aryl sulfotransferase 2, Phenol sulfotransferase 2, and Phenol-sulfating phenol sulfotransferase 2, plays a pivotal role in the metabolism of various substances. It utilizes 3'-phospho-5'-adenylyl sulfate as a sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs, and neurotransmitters. Additionally, it is crucial for the sulfonation and activation of minoxidil and mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products.
Therapeutic significance:
Understanding the role of Sulfotransferase 1A2 could open doors to potential therapeutic strategies, especially in the context of its involvement in drug metabolism and potential modulation of cancer risk.