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.
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 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.
Our high-tech, dedicated method is applied to construct targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The method includes detailed molecular simulations of the catalytic and allosteric binding pockets, along with ensemble virtual screening that considers their conformational flexibility. In the design of modulators, structural changes induced by reaction intermediates are taken into account to enhance activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q8N3T1
UPID:
GLT15_HUMAN
Alternative names:
Polypeptide GalNAc transferase-like protein 2; Polypeptide N-acetylgalactosaminyltransferase-like protein 2; Protein-UDP acetylgalactosaminyltransferase-like protein 2; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
Alternative UPACC:
Q8N3T1; A6NMN1; B2R638; F1LIP6; Q86T60; Q96C46; Q96DJ5
Background:
Polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) plays a crucial role in the biosynthesis of O-linked oligosaccharides by transferring N-acetyl-D-galactosamine to serine or threonine residues on proteins. Despite its weaker activity compared to GALNT2, GALNT15 can add multiple GalNAc residues to the Muc5AC peptide, indicating its ability to work alongside other GALNT proteins and showing a preference for Muc1a as a substrate.
Therapeutic significance:
Understanding the role of Polypeptide N-acetylgalactosaminyltransferase 15 could open doors to potential therapeutic strategies.