Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced 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.
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.
Our high-tech, dedicated method is applied to construct targeted libraries.
Fig. 1. The sreening workflow of Receptor.AI
Utilising molecular simulations, our approach thoroughly examines a wide array of proteins, tracking their conformational changes individually and within complexes. Ensemble virtual screening enables us to address conformational flexibility, revealing essential binding sites at functional regions and allosteric locations. Our rigorous analysis guarantees that no potential mechanism of action is overlooked, aiming to uncover new therapeutic targets and lead compounds across diverse biological functions.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q53H47
UPID:
SETMR_HUMAN
Alternative names:
SET domain and mariner transposase fusion protein
Alternative UPACC:
Q53H47; B4DY74; E7EN68; Q13579; Q1G668; Q96F41
Background:
Histone-lysine N-methyltransferase SETMAR, derived from the fusion of a methylase with the transposase of an Hsmar1 transposon, plays a crucial role in DNA repair, replication fork restart, and DNA integration. It binds DNA, recognizing the 19-mer core of Hsmar1 element's 5'-terminal inverted repeats, and exhibits DNA nicking and end joining activity. Additionally, SETMAR methylates 'Lys-4' and 'Lys-36' of histone H3, mediating dimethylation at DNA double-strand break sites, potentially recruiting proteins for DSB repair.
Therapeutic significance:
Understanding the role of Histone-lysine N-methyltransferase SETMAR could open doors to potential therapeutic strategies.