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.
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.
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 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 is unique due to several crucial aspects:
partner
Reaxense
upacc
O60502
UPID:
OGA_HUMAN
Alternative names:
Beta-N-acetylglucosaminidase; Beta-N-acetylhexosaminidase; Beta-hexosaminidase; Meningioma-expressed antigen 5; N-acetyl-beta-D-glucosaminidase; N-acetyl-beta-glucosaminidase; Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
Alternative UPACC:
O60502; B7WPB9; D3DR79; E9PGF9; O75166; Q86WV0; Q8IV98; Q9BVA5; Q9HAR0
Background:
Protein O-GlcNAcase, also known as Beta-N-acetylglucosaminidase, plays a crucial role in the cleavage of GlcNAc from O-glycosylated proteins. This enzyme exhibits specificity by targeting p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates, showcasing its unique enzymatic activity. It is distinguished by its inability to cleave GalNAc or bind acetyl-CoA, highlighting its specialized function in cellular processes.
Therapeutic significance:
Understanding the role of Protein O-GlcNAcase could open doors to potential therapeutic strategies. Its specific enzymatic activity in processing O-glycosylated proteins underlines its importance in cellular mechanisms, suggesting its potential as a target in therapeutic interventions.