Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved 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.
We use our state-of-the-art dedicated workflow for designing focused libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The method includes detailed molecular simulations of the catalytic and allosteric binding pockets, along with ensemble virtual screening that considers their conformational flexibility. In the design of modulators, structural changes induced by reaction intermediates are taken into account to enhance activity and selectivity.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
Q12797
UPID:
ASPH_HUMAN
Alternative names:
Aspartate beta-hydroxylase; Peptide-aspartate beta-dioxygenase
Alternative UPACC:
Q12797; A0A0A0MSK8; A6NDF4; A6NHI2; B4DIC9; B4E2K4; B7ZM95; E5RGP5; F5H667; Q6NXR7; Q8TB28; Q9H291; Q9H2C4; Q9NRI0; Q9NRI1; Q9Y4J0
Background:
Aspartyl/asparaginyl beta-hydroxylase, also known as Aspartate beta-hydroxylase or Peptide-aspartate beta-dioxygenase, plays a crucial role in modifying certain epidermal growth factor-like domains. This modification involves the hydroxylation of Asp or Asn residues, which is essential for protein function. Additionally, it acts as a membrane-bound Ca(2+)-sensing protein, contributing to the structure of ER-plasma membrane junctions and regulating T-cell activity.
Therapeutic significance:
The protein is implicated in a rare syndrome characterized by facial dysmorphism, lens dislocation, and anterior segment abnormalities. Understanding the role of Aspartyl/asparaginyl beta-hydroxylase could open doors to potential therapeutic strategies for this condition.