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 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.
We employ our advanced, specialised process to create targeted 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
Q86Y97
UPID:
KMT5C_HUMAN
Alternative names:
Lysine N-methyltransferase 5C; Lysine-specific methyltransferase 5C; Suppressor of variegation 4-20 homolog 2; [histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B; [histone H4]-lysine20 N-methyltransferase KMT5B
Alternative UPACC:
Q86Y97; Q8WZ10; Q9BRZ6
Background:
Histone-lysine N-methyltransferase KMT5C, also known as Lysine N-methyltransferase 5C, plays a pivotal role in histone modification, specifically targeting the 'Lys-20' site on histone H4. This enzyme is crucial for the methylation process, converting monomethylated and dimethylated 'Lys-20' to dimethylated and trimethylated forms, respectively. Such modifications are essential for transcription regulation and maintaining genome integrity. KMT5C's activity is not limited to histones but extends to nucleosomes, indicating its broad role in epigenetic transcriptional repression and DNA repair mechanisms.
Therapeutic significance:
Understanding the role of Histone-lysine N-methyltransferase KMT5C could open doors to potential therapeutic strategies.