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.
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.
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 comprehensive molecular simulations of the catalytic and allosteric binding pockets and the ensemble virtual screening accounting for their conformational mobility. In the case of designing modulators, the structural changes induced by reaction intermediates are taken into account to leverage activity and selectivity.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
Q9HAC7
UPID:
SUCHY_HUMAN
Alternative names:
Dermal papilla-derived protein 13; SuccinylCoA:glutarate-CoA transferase
Alternative UPACC:
Q9HAC7; A4D1W5; B4DR73; Q4KMW4; Q4KMW8; Q4KMZ0; Q8TE00; Q8TEY1
Background:
Succinate--hydroxymethylglutarate CoA-transferase, also known as Dermal papilla-derived protein 13, plays a crucial role in metabolic pathways by catalyzing the succinyl-CoA-dependent conversion of glutarate to glutaryl-CoA. It exhibits versatility in using different dicarboxylic acids as CoA acceptors, with a preference for glutarate, succinate, adipate, and 3-hydroxymethylglutarate.
Therapeutic significance:
This protein's malfunction is linked to Glutaric aciduria 3, a metabolic disorder stemming from peroxisomal glutaryl-CoA oxidase deficiency. Understanding the role of Succinate--hydroxymethylglutarate CoA-transferase could open doors to potential therapeutic strategies for this condition.