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.
We carefully select specific compounds from a vast collection of over 60 billion molecules in virtual chemical space. Our partner Reaxense helps in synthesizing and delivering these compounds.
The library includes a list of the most promising modulators annotated with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Also, each compound is presented with its optimal docking poses, affinity scores, and activity scores, providing a comprehensive overview.
We utilise our cutting-edge, exclusive workflow to develop focused 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.
Several key aspects differentiate our library:
partner
Reaxense
upacc
Q9BV81
UPID:
EMC6_HUMAN
Alternative names:
Transmembrane protein 93
Alternative UPACC:
Q9BV81
Background:
ER membrane protein complex subunit 6, also known as Transmembrane protein 93, is integral to the endoplasmic reticulum membrane protein complex (EMC). It plays a crucial role in the insertion of newly synthesized membrane proteins into the endoplasmic reticulum membranes without energy dependency. This protein is adept at accommodating proteins with transmembrane domains that are less hydrophobic or have destabilizing features, including charged and aromatic residues. It is essential for the cotranslational and post-translational insertion of multi-pass and tail-anchored proteins into the ER membrane, influencing the topology of multi-pass membrane proteins like G protein-coupled receptors.
Therapeutic significance:
Understanding the role of ER membrane protein complex subunit 6 could open doors to potential therapeutic strategies.