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 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.
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 for enzymes.
Fig. 1. The sreening workflow of Receptor.AI
The procedure entails thorough molecular simulations of the catalytic and allosteric binding pockets, accompanied by ensemble virtual screening that factors in their conformational flexibility. When developing modulators, the structural modifications brought about by reaction intermediates are factored in to optimize activity and selectivity.
Several key aspects differentiate our library:
partner
Reaxense
upacc
P30419
UPID:
NMT1_HUMAN
Alternative names:
Myristoyl-CoA:protein N-myristoyltransferase 1; Peptide N-myristoyltransferase 1; Protein-lysine myristoyltransferase NMT1
Alternative UPACC:
P30419; A8K7C1; Q9UE09
Background:
Glycylpeptide N-tetradecanoyltransferase 1, also known as Myristoyl-CoA:protein N-myristoyltransferase 1, plays a crucial role in the post-translational modification of proteins. It specifically adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins, enhancing their function and interaction with cellular membranes. This enzyme is also capable of mediating N-terminal lysine myristoylation, a modification essential for the proper membrane association of proteins such as ARF6.
Therapeutic significance:
Understanding the role of Glycylpeptide N-tetradecanoyltransferase 1 could open doors to potential therapeutic strategies.