Focused On-demand Library for All trans-polyprenyl-diphosphate synthase PDSS2

Available from Reaxense
Predicted by Alphafold

Focused On-demand Libraries - Reaxense Collaboration

Explore the Potential with AI-Driven Innovation

The focused library is created on demand with the latest virtual screening and parameter assessment technology, supported by the Receptor.AI drug discovery platform. This method is more effective than traditional methods and results in higher-quality compounds with better 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.

In the library, a selection of top modulators is provided, each marked with 38 ADME-Tox and 32 parameters related to physicochemical properties and drug-likeness. Also, every compound comes with its best docking poses, affinity scores, and activity scores, providing a comprehensive overview.

Our top-notch dedicated system is used to design specialised libraries.

 Fig. 1. The sreening workflow of Receptor.AI

By deploying molecular simulations, our approach comprehensively covers a broad array of proteins, tracking their flexibility and dynamics individually and within complexes. Ensemble virtual screening is utilised to take into account conformational dynamics, identifying pivotal binding sites located within functional regions and at allosteric locations. This thorough exploration ensures that every conceivable mechanism of action is considered, aiming to identify new therapeutic targets and advance lead compounds throughout a vast spectrum of biological functions.

Our library is unique due to several crucial aspects:

  • Receptor.AI compiles all relevant data on the target protein, such as past experimental results, literature findings, known ligands, and structural data, thereby enhancing the likelihood of focusing on the most significant compounds.
  • By utilizing advanced molecular simulations, the platform is adept at locating potential binding sites, rendering the compounds in the focused library well-suited for unearthing allosteric inhibitors and binders for hidden pockets.
  • The platform is supported by more than 50 highly specialized AI models, all of which have been rigorously tested and validated in diverse drug discovery and research programs. Its design emphasizes efficiency, reliability, and accuracy, crucial for producing focused libraries.
  • Receptor.AI extends beyond just creating focused libraries; it offers a complete spectrum of services and solutions during the preclinical drug discovery phase, with a success-dependent pricing strategy that reduces risk and fosters shared success in the project.







Alternative names:

All-trans-decaprenyl-diphosphate synthase subunit 2; Candidate tumor suppressor protein; Decaprenyl pyrophosphate synthase subunit 2; Decaprenyl-diphosphate synthase subunit 2; Solanesyl-diphosphate synthase subunit 2

Alternative UPACC:

Q86YH6; Q33DR4; Q4G158; Q5VU38; Q5VU39; Q9NR58


All trans-polyprenyl-diphosphate synthase PDSS2, also known as Decaprenyl-diphosphate synthase subunit 2, plays a crucial role in the biosynthesis of coenzyme Q10 (CoQ10). This enzyme catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to produce prenyl diphosphates, essential for CoQ10 synthesis. CoQ10 is vital for mitochondrial respiratory chain function and cellular energy production.

Therapeutic significance:

Mutations in PDSS2 are linked to Coenzyme Q10 deficiency, primary, 3, a fatal disorder affecting the brain, muscles, and kidneys. Understanding PDSS2's role could lead to novel treatments for this and related mitochondrial diseases, highlighting its potential in therapeutic strategies.

Looking for more information on this library or underlying technology? Fill out the form below and we'll be in touch with all the details you need.
Thank you! Your submission has been received!
Oops! Something went wrong while submitting the form.