Explore the Potential with AI-Driven Innovation
Our detailed focused library is generated on demand with advanced virtual screening and parameter assessment technology powered by the Receptor.AI drug discovery platform. This method surpasses traditional approaches, delivering compounds of better quality with enhanced 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 top-notch dedicated system is used to design specialised libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Our library is unique due to several crucial aspects:
partner
Reaxense
upacc
P61956
UPID:
SUMO2_HUMAN
Alternative names:
HSMT3; SMT3 homolog 2; SUMO-3; Sentrin-2; Ubiquitin-like protein SMT3B
Alternative UPACC:
P61956; B2R4I2; P55855; Q32Q42; Q6IPZ6; Q96HK1
Background:
Small ubiquitin-related modifier 2 (SUMO-2), known by alternative names such as HSMT3, SMT3 homolog 2, and Sentrin-2, plays a pivotal role in cellular processes. It is involved in nuclear transport, DNA replication and repair, mitosis, and signal transduction through its covalent attachment to proteins. This modification, which can occur as a monomer or lysine-linked polymer, is facilitated by a series of enzymes including SAE1-SAE2, UBE2I, and E3 ligases like PIAS1-4.
Therapeutic significance:
Understanding the role of Small ubiquitin-related modifier 2 could open doors to potential therapeutic strategies.