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.
The compounds are cherry-picked from the vast virtual chemical space of over 60B molecules. The synthesis and delivery of compounds is facilitated by our partner Reaxense.
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.
We utilise our cutting-edge, exclusive workflow to develop focused 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
Q9Y530
UPID:
OARD1_HUMAN
Alternative names:
O-acetyl-ADP-ribose deacetylase 1; Terminal ADP-ribose protein glycohydrolase 1; [Protein ADP-ribosylglutamate] hydrolase OARD1
Alternative UPACC:
Q9Y530; A6NEK4; A8K4H4; Q96F23
Background:
ADP-ribose glycohydrolase OARD1, known alternatively as O-acetyl-ADP-ribose deacetylase 1, Terminal ADP-ribose protein glycohydrolase 1, and [Protein ADP-ribosylglutamate] hydrolase OARD1, plays a crucial role in cellular processes. It hydrolyzes ADP-ribose, acting on substrates like proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose. OARD1 specifically acts as a glutamate mono-ADP-ribosylhydrolase, removing mono-ADP-ribose attached to glutamate residues on proteins. It does not act on poly-ADP-ribosylated proteins but can deacetylate O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.
Therapeutic significance:
Understanding the role of ADP-ribose glycohydrolase OARD1 could open doors to potential therapeutic strategies.