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.
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 features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
Our high-tech, dedicated method is applied to construct targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
This approach involves comprehensive molecular simulations of the catalytic and allosteric binding pockets and ensemble virtual screening that accounts for their conformational flexibility. In the case of designing modulators, the structural adjustments caused by reaction intermediates are considered to improve activity and selectivity.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
Q96EY8
UPID:
MMAB_HUMAN
Alternative names:
ATP:co(I)rrinoid adenosyltransferase MMAB; Methylmalonic aciduria type B protein
Alternative UPACC:
Q96EY8; C5HU05; Q9BSH0
Background:
Corrinoid adenosyltransferase MMAB, also known as ATP:co(I)rrinoid adenosyltransferase and Methylmalonic aciduria type B protein, plays a pivotal role in vitamin B12 metabolism. It converts cob(I)alamin into adenosylcobalamin (AdoCbl), a crucial coenzyme for methylmalonyl-CoA mutase. This process is essential for the final step of vitamin B12 conversion, highlighting the protein's significance in metabolic pathways.
Therapeutic significance:
Given its critical role in the metabolism of methylmalonate and cobalamin, MMAB is directly linked to Methylmalonic aciduria type cblB, a metabolic disorder. Understanding the function of Corrinoid adenosyltransferase MMAB could open doors to potential therapeutic strategies for treating this condition by targeting the underlying genetic variants.