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.
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.
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 employ our advanced, specialised process to create targeted libraries for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The method includes detailed molecular simulations of the catalytic and allosteric binding pockets, along with ensemble virtual screening that considers their conformational flexibility. In the design of modulators, structural changes induced by reaction intermediates are taken into account to enhance activity and selectivity.
Key features that set our library apart include:
partner
Reaxense
upacc
P0C870
UPID:
JMJD7_HUMAN
Alternative names:
JmjC domain-containing protein 7; Jumonji domain-containing protein 7; L-lysine (3S)-hydroxylase JMJD7
Alternative UPACC:
P0C870; A5D6V5; O95712; Q59GF9; Q8TB10; Q9UKV7
Background:
Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7, also known as JmjC domain-containing protein 7, plays a crucial role in histone modification and protein biosynthesis. It acts as an endopeptidase, cleaving histones' N-terminal tails, and as a monooxygenase, hydroxylating specific lysine residues on translation factors. This dual functionality underscores its importance in transcription regulation and protein synthesis.
Therapeutic significance:
Understanding the role of Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7 could open doors to potential therapeutic strategies.