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.
The compounds are cherry-picked from the vast virtual chemical space of over 60B molecules. The synthesis and delivery of compounds is facilitated by our partner Reaxense.
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 utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Utilising molecular simulations, our approach thoroughly examines a wide array of proteins, tracking their conformational changes individually and within complexes. Ensemble virtual screening enables us to address conformational flexibility, revealing essential binding sites at functional regions and allosteric locations. Our rigorous analysis guarantees that no potential mechanism of action is overlooked, aiming to uncover new therapeutic targets and lead compounds across diverse biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q14165
UPID:
MLEC_HUMAN
Alternative names:
-
Alternative UPACC:
Q14165
Background:
Malectin is a carbohydrate-binding protein with a preference for Glc2-N-glycan, suggesting a specialized role in protein N-glycosylation. This process is crucial for protein folding and stability, indicating Malectin's importance in cellular functions.
Therapeutic significance:
Understanding the role of Malectin could open doors to potential therapeutic strategies. Its involvement in protein glycosylation, a process critical for protein function and stability, highlights its potential as a target in diseases where glycosylation patterns are disrupted.