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 includes a list of the most promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
Our top-notch dedicated system is used to design specialised 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 distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q9Y672
UPID:
ALG6_HUMAN
Alternative names:
Asparagine-linked glycosylation protein 6 homolog; Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase; Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
Alternative UPACC:
Q9Y672; B3KMU2; Q5SXR9; Q9H3I0
Background:
Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase, also known as Asparagine-linked glycosylation protein 6 homolog, plays a pivotal role in the process of N-linked glycosylation. It is responsible for adding the first glucose residue to the lipid-linked oligosaccharide precursor, a critical step in the biosynthesis of glycoproteins.
Therapeutic significance:
The protein's malfunction is linked to Congenital disorder of glycosylation 1C, a condition with a wide range of clinical features including developmental and immunological defects. Understanding the role of Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase could open doors to potential therapeutic strategies for this multisystem disorder.