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.
We pick out particular compounds from an extensive virtual database of more than 60 billion molecules. The preparation and shipment of these compounds are facilitated by our associate Reaxense.
The library features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
Our high-tech, dedicated method is applied to construct targeted libraries.
Fig. 1. The sreening workflow of Receptor.AI
By deploying molecular simulations, our approach comprehensively covers a broad array of proteins, tracking their flexibility and dynamics individually and within complexes. Ensemble virtual screening is utilised to take into account conformational dynamics, identifying pivotal binding sites located within functional regions and at allosteric locations. This thorough exploration ensures that every conceivable mechanism of action is considered, aiming to identify new therapeutic targets and advance lead compounds throughout a vast spectrum of biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q8IWU5
UPID:
SULF2_HUMAN
Alternative names:
Arylsulfatase; N-acetylglucosamine-6-sulfatase
Alternative UPACC:
Q8IWU5; E1P5U6; Q5JYE1; Q6UX86; Q96SG2; Q9H1H0; Q9UJR3; Q9ULH3
Background:
Extracellular sulfatase Sulf-2, known for its arylsulfatase and highly specific endoglucosamine-6-sulfatase activity, plays a pivotal role in modifying the sulfation patterns of heparin. This modification process is crucial for the regulation of various biological activities, as it involves the removal of sulfate from the C-6 position of glucosamine within specific subregions of intact heparin.
Therapeutic significance:
Understanding the role of Extracellular sulfatase Sulf-2 could open doors to potential therapeutic strategies. Its unique enzymatic activities suggest its involvement in critical biological processes, making it a target of interest for drug discovery efforts aimed at modulating heparin-related functions.