Explore the Potential with AI-Driven Innovation
This comprehensive focused library is produced on demand with state-of-the-art virtual screening and parameter assessment technology driven by Receptor.AI drug discovery platform. This approach outperforms traditional methods and provides higher-quality compounds with superior 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.
In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We employ our advanced, specialised process to create targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
It includes in-depth molecular simulations of both the catalytic and allosteric binding pockets, with ensemble virtual screening focusing on their conformational flexibility. For modulators, the process includes considering the structural shifts due to reaction intermediates to boost activity and selectivity.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q400G9
UPID:
AMZ1_HUMAN
Alternative names:
Archeobacterial metalloproteinase-like protein 1
Alternative UPACC:
Q400G9; B3KRS0; Q8TF51
Background:
Archaemetzincin-1, also known as Archeobacterial metalloproteinase-like protein 1, is identified as a probable zinc metalloprotease. This classification suggests its involvement in catalyzing the cleavage of peptide bonds in proteins, a critical process in various biological functions. The protein's unique structure and enzymatic capabilities position it as a significant subject for in-depth biochemical research.
Therapeutic significance:
Understanding the role of Archaemetzincin-1 could open doors to potential therapeutic strategies. Its enzymatic function as a metalloprotease indicates its potential involvement in key biological processes, which, if modulated, could lead to novel treatments for diseases where protease activity is dysregulated.