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.
From a virtual chemical space containing more than 60 billion molecules, we precisely choose certain compounds. Our collaborator, Reaxense, aids in their synthesis and provision.
The library features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
We utilise our cutting-edge, exclusive workflow to develop focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
This approach involves comprehensive molecular simulations of the catalytic and allosteric binding pockets and ensemble virtual screening that accounts for their conformational flexibility. In the case of designing modulators, the structural adjustments caused by reaction intermediates are considered to improve activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
O60507
UPID:
TPST1_HUMAN
Alternative names:
Tyrosylprotein sulfotransferase 1
Alternative UPACC:
O60507; A4D2M0; Q6FGM7
Background:
Protein-tyrosine sulfotransferase 1, alternatively known as Tyrosylprotein sulfotransferase 1, plays a crucial role in post-translational modifications by catalyzing the O-sulfation of tyrosine residues within acidic motifs of polypeptides. This process utilizes 3'-phosphoadenylyl sulfate (PAPS) as a cosubstrate, highlighting its significance in protein function and signaling pathways.
Therapeutic significance:
Understanding the role of Protein-tyrosine sulfotransferase 1 could open doors to potential therapeutic strategies. Its involvement in critical post-translational modifications suggests that modulating its activity could have implications for diseases where these processes are dysregulated.