Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior 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.
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.
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.
Several key aspects differentiate our library:
partner
Reaxense
upacc
P54793
UPID:
ARSF_HUMAN
Alternative names:
-
Alternative UPACC:
P54793; Q8TCC5
Background:
Arylsulfatase F, encoded by the gene with the accession number P54793, plays a crucial role in cellular processes by exhibiting arylsulfatase activity towards the artificial substrate 4-methylumbelliferyl sulfate. This enzyme is part of a larger family of arylsulfatases, which are known for their ability to hydrolyze sulfate esters, a vital function in the degradation of sulfated glycosaminoglycans.
Therapeutic significance:
Understanding the role of Arylsulfatase F could open doors to potential therapeutic strategies. Its enzymatic activity suggests a fundamental role in cellular metabolism and degradation processes, which, if dysregulated, could lead to disease states. Investigating Arylsulfatase F further could unveil novel therapeutic targets.