Explore the Potential with AI-Driven Innovation
The focused library is created on demand with the latest virtual screening and parameter assessment technology, supported by the Receptor.AI drug discovery platform. This method is more effective than traditional methods and results in higher-quality compounds with better 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 high-tech, dedicated method is applied to construct targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes comprehensive molecular simulations of the catalytic and allosteric binding pockets and the ensemble virtual screening accounting for their conformational mobility. In the case of designing modulators, the structural changes induced by reaction intermediates are taken into account to leverage activity and selectivity.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
O15305
UPID:
PMM2_HUMAN
Alternative names:
-
Alternative UPACC:
O15305; A8K672; B7Z6R0; D3DUF3
Background:
Phosphomannomutase 2 (PMM2) plays a pivotal role in the synthesis of GDP-mannose and dolichol-phosphate-mannose, essential for numerous mannosyl transfer reactions. These reactions are crucial for proper glycoprotein biosynthesis, impacting a wide array of cellular functions and developmental processes.
Therapeutic significance:
PMM2's dysfunction is linked to Congenital disorder of glycosylation 1A (CDG1A), a severe condition marked by encephalopathy, psychomotor retardation, and other systemic manifestations. Understanding the role of Phosphomannomutase 2 could open doors to potential therapeutic strategies for CDG1A and related glycosylation disorders.