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.
From a virtual chemical space containing more than 60 billion molecules, we precisely choose certain compounds. Our collaborator, Reaxense, aids in their synthesis and provision.
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.
Our high-tech, dedicated method is applied to construct targeted libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our strategy employs molecular simulations to explore an extensive range of proteins, capturing their dynamics both individually and within complexes with other proteins. Through ensemble virtual screening, we address proteins' conformational mobility, uncovering key binding sites at both functional regions and remote allosteric locations. This comprehensive investigation ensures a thorough assessment of all potential mechanisms of action, with the goal of discovering innovative therapeutic targets and lead molecules across across diverse biological functions.
Our library distinguishes itself through several key aspects:
partner
Reaxense
upacc
P04843
UPID:
RPN1_HUMAN
Alternative names:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit; Ribophorin I; Ribophorin-1
Alternative UPACC:
P04843; B2R5Z0; D3DNB6; Q68DT1
Background:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1, also known as Ribophorin I or Ribophorin-1, plays a crucial role in protein N-glycosylation. This process involves the transfer of a specific glycan from dolichol-pyrophosphate to an asparagine residue within nascent polypeptide chains. It occurs cotranslationally and is essential for protein folding and stability. The protein is part of the oligosaccharyl transferase (OST) complex, which associates with the Sec61 complex at the ER translocon, facilitating protein translocation across the endoplasmic reticulum.
Therapeutic significance:
Understanding the role of Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 could open doors to potential therapeutic strategies.