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 employ our advanced, specialised process to create targeted 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.
Several key aspects differentiate our library:
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.