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.
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.
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.
We use our state-of-the-art dedicated workflow for designing focused 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
Q8NBK3
UPID:
SUMF1_HUMAN
Alternative names:
C-alpha-formylglycine-generating enzyme 1; Sulfatase-modifying factor 1
Alternative UPACC:
Q8NBK3; B4DXK5; B7XD05; E9PGL0; G5E9B0; Q0VAC6; Q0VAC7; Q2NL78; Q53ZE4; Q6UY39; Q96AK5; Q96DK8
Background:
The Formylglycine-generating enzyme, also known as C-alpha-formylglycine-generating enzyme 1 or Sulfatase-modifying factor 1, plays a pivotal role in the post-translational modification of sulfatases. It catalyzes the conversion of cysteine to 3-oxoalanine (formylglycine), a critical step in the activation of several sulfatases, including arylsulfatases and alkaline phosphatases.
Therapeutic significance:
Multiple sulfatase deficiency, a disorder resulting from mutations in the SUMF1 gene, underscores the enzyme's crucial role. This condition highlights the enzyme's potential as a target for therapeutic intervention, aiming to correct the underlying genetic and biochemical defects.