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.
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.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
We use our state-of-the-art dedicated workflow for designing focused 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.
Key features that set our library apart include:
partner
Reaxense
upacc
Q5T6V5
UPID:
QNG1_HUMAN
Alternative names:
Q-nucleotide N-glycosylase 1; Queuine salvage protein QNG1; Queuosine-nucleotide N-glycosylase/hydrolase
Alternative UPACC:
Q5T6V5; B2RPI6; Q8N2B1; Q9BT18
Background:
Queuosine 5'-phosphate N-glycosylase/hydrolase, also known as Q-nucleotide N-glycosylase 1 or Queuine salvage protein QNG1, plays a crucial role in the metabolism of queuosine (Q), a modified nucleobase found in tRNA. It catalyzes the hydrolysis of queuosine 5'-phosphate, facilitating the salvage of queuine from exogenous sources. This enzyme exhibits specificity for the queuine base, underscoring its unique function in cellular processes.
Therapeutic significance:
Understanding the role of Queuosine 5'-phosphate N-glycosylase/hydrolase could open doors to potential therapeutic strategies.