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.
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.
We use our state-of-the-art dedicated workflow for designing focused 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 distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q8N4A0
UPID:
GALT4_HUMAN
Alternative names:
Polypeptide GalNAc transferase 4; Protein-UDP acetylgalactosaminyltransferase 4; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Alternative UPACC:
Q8N4A0; B2R775; B4DMX6; O00208
Background:
Polypeptide N-acetylgalactosaminyltransferase 4, also known as Protein-UDP acetylgalactosaminyltransferase 4 or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4, plays a crucial role in the biosynthesis of O-linked oligosaccharides. It catalyzes the transfer of an N-acetyl-D-galactosamine residue to serine or threonine residues on protein receptors, showing highest activity towards Muc7, EA2, and Muc2.
Therapeutic significance:
Understanding the role of Polypeptide N-acetylgalactosaminyltransferase 4 could open doors to potential therapeutic strategies.