Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior 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.
In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q9NZL9
UPID:
MAT2B_HUMAN
Alternative names:
Methionine adenosyltransferase II beta; Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase
Alternative UPACC:
Q9NZL9; B2R5Y6; Q1WAI7; Q27J92; Q3LIE8; Q567T7; Q6NYC7; Q9BS89; Q9H3E1; Q9UJ54
Background:
Methionine adenosyltransferase 2 subunit beta, also known as Methionine adenosyltransferase II beta, plays a crucial role as a regulatory subunit of S-adenosylmethionine synthetase 2. This enzyme is pivotal in catalyzing the formation of S-adenosylmethionine from methionine and ATP, with the protein enhancing MAT2A's affinity for L-methionine. Additionally, it has been shown to bind NADP in vitro, indicating a versatile function in cellular metabolism.
Therapeutic significance:
Understanding the role of Methionine adenosyltransferase 2 subunit beta could open doors to potential therapeutic strategies.