ProxyBind

ProxyBind surveys the human proteome to identify non-catalytic drug binding pockets within protein-modifying enzymes using structural data from the Protein Databank for proximity-induced pharmacology.

Key Features:

• Proteome-wide survey: Systematically surveys the human proteome to locate candidate sites for proximity pharmacology.
• Non-catalytic pocket identification: Identifies non-catalytic drug binding pockets within protein-modifying enzymes.
• Structural data integration: Analyzes structures from the Protein Databank to detect ligandable cavities.
• Enzyme class coverage: Reveals putative ligandable sites across kinases, phosphatases, deubiquitinases, methyltransferases, acetyltransferases, glycosyltransferases, deacetylases, and demethylases.

Scientific Applications:

• New Drug Targets: Expands opportunities to pharmacologically modulate molecular interactions by identifying novel cavities accessible to chemical matter.

Methodology:

Surveys the human proteome and maps binding sites by analyzing Protein Databank structures to identify non-catalytic ligandable pockets in protein-modifying enzymes.