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.
We carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
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
It includes in-depth molecular simulations of both the catalytic and allosteric binding pockets, with ensemble virtual screening focusing on their conformational flexibility. For modulators, the process includes considering the structural shifts due to reaction intermediates to boost activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
O60547
UPID:
GMDS_HUMAN
Alternative names:
GDP-D-mannose dehydratase
Alternative UPACC:
O60547; E9PI88; O75357; Q5T954; Q6FH09; Q9UGZ3; Q9UJK9
Background:
GDP-mannose 4,6 dehydratase, also known as GDP-D-mannose dehydratase, plays a pivotal role in the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. This enzyme is crucial in the biosynthesis pathway of GDP-fucose, a donor substrate for fucosylation processes, which are essential for cell-cell interaction and communication.
Therapeutic significance:
Understanding the role of GDP-mannose 4,6 dehydratase could open doors to potential therapeutic strategies. Its involvement in the biosynthesis of key sugars suggests a foundational role in cellular functions and potential implications in diseases where fucosylation patterns are disrupted.