Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved activity, selectivity, and safety.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner Reaxense.
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.
We utilise our cutting-edge, exclusive workflow to develop focused 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.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q8TCJ2
UPID:
STT3B_HUMAN
Alternative names:
Source of immunodominant MHC-associated peptides homolog
Alternative UPACC:
Q8TCJ2; Q96JZ4; Q96KY7
Background:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B plays a pivotal role in protein N-glycosylation, a process critical for protein folding and stability. It acts as the catalytic subunit within the oligosaccharyl transferase complex, facilitating the transfer of glycan chains to nascent proteins, essential for their proper function and localization. Its activity is crucial in both co- and post-translational modifications, impacting a wide array of biological processes.
Therapeutic significance:
Given its central role in glycoprotein biosynthesis, STT3B's dysfunction is linked to Congenital disorder of glycosylation 1X, manifesting in severe developmental and systemic anomalies. Understanding the role of STT3B could open doors to potential therapeutic strategies, offering hope for targeted interventions in glycosylation disorders and enhancing our approach to precision medicine.