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.
From a virtual chemical space containing more than 60 billion molecules, we precisely choose certain compounds. Our collaborator, Reaxense, aids in their synthesis and provision.
The library includes a list of the most effective modulators, each annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Furthermore, each compound is shown with its optimal docking poses, affinity scores, and activity scores, offering a detailed summary.
Our high-tech, dedicated method is applied to construct targeted libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology employs molecular simulations to explore a wide array of proteins, capturing their dynamic states both individually and within complexes. Through ensemble virtual screening, we address conformational mobility, uncovering binding sites within functional regions and remote allosteric locations. This thorough exploration ensures no potential mechanism of action is overlooked, aiming to discover novel therapeutic targets and lead compounds across an extensive spectrum of biological functions.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
Q9NV79
UPID:
PCMD2_HUMAN
Alternative names:
-
Alternative UPACC:
Q9NV79; E1P5H3; Q8IW60; Q9H4K2
Background:
Protein-L-isoaspartate O-methyltransferase domain-containing protein 2, identified by the accession number Q9NV79, plays a crucial role in cellular processes through its involvement in the ECS (Elongin BC-CUL5-SOCS-box protein) E3 ubiquitin ligase complex. This complex is pivotal for the ubiquitination and subsequent proteasomal degradation of target proteins. Despite its name suggesting a potential enzymatic activity, this protein likely does not exhibit methyltransferase activity but is thought to interact with the methyltransferase cofactor S-adenosylmethionine (AdoMet) through its N-terminal AdoMet binding motif.
Therapeutic significance:
Understanding the role of Protein-L-isoaspartate O-methyltransferase domain-containing protein 2 could open doors to potential therapeutic strategies.