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.
The library features a range of promising modulators, each detailed with 38 ADME-Tox and 32 physicochemical and drug-likeness parameters. Plus, each compound is presented with its ideal docking poses, affinity scores, and activity scores, ensuring a thorough insight.
We utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology employs molecular simulations to explore a wide array of proteins, capturing their dynamic states both individually and within complexes. Through ensemble virtual screening, we address conformational mobility, uncovering binding sites within functional regions and remote allosteric locations. This thorough exploration ensures no potential mechanism of action is overlooked, aiming to discover novel therapeutic targets and lead compounds across an extensive spectrum of biological functions.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q8N4V1
UPID:
EMC5_HUMAN
Alternative names:
Membrane magnesium transporter 1; Transmembrane protein 32
Alternative UPACC:
Q8N4V1; B2R625; B4DIY3; D3DWG7; Q5JPP7
Background:
ER membrane protein complex subunit 5, also known as Membrane magnesium transporter 1 and Transmembrane protein 32, is integral to the endoplasmic reticulum membrane protein complex (EMC). It facilitates the insertion of newly synthesized membrane proteins into endoplasmic reticulum membranes without energy input. This protein is adept at handling proteins with transmembrane domains that are less hydrophobic or have destabilizing features. It plays a crucial role in the cotranslational and post-translational insertion of multi-pass and tail-anchored proteins, respectively, and is essential for the correct topology of multi-pass membrane proteins like G protein-coupled receptors.
Therapeutic significance:
Understanding the role of ER membrane protein complex subunit 5 could open doors to potential therapeutic strategies.