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.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner Reaxense.
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 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 distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q8TBC4
UPID:
UBA3_HUMAN
Alternative names:
NEDD8-activating enzyme E1C; Ubiquitin-activating enzyme E1C; Ubiquitin-like modifier-activating enzyme 3
Alternative UPACC:
Q8TBC4; A6NLB5; A8K027; O76088; Q9NTU3
Background:
The NEDD8-activating enzyme E1 catalytic subunit, known alternatively as NEDD8-activating enzyme E1C, Ubiquitin-activating enzyme E1C, or Ubiquitin-like modifier-activating enzyme 3, plays a pivotal role in protein modification. It is the catalytic subunit of the UBA3-NAE1 E1 enzyme, essential for activating NEDD8, a process crucial for cell cycle progression and down-regulating steroid receptor activity.
Therapeutic significance:
Understanding the role of NEDD8-activating enzyme E1 catalytic subunit could open doors to potential therapeutic strategies.