Explore the Potential with AI-Driven Innovation
The specialised, focused library is developed on demand with the most recent virtual screening and parameter assessment technology, guided by the Receptor.AI drug discovery platform. This approach exceeds the capabilities of traditional methods and offers compounds with higher 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.
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.
Several key aspects differentiate our library:
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.