MOAD

MOAD curates a large collection of high-quality x-ray crystal structures of protein–ligand complexes and associated experimental binding affinities to support polypharmacology analysis and drug repurposing.

Key Features:

• Structure collection: Curates 32,747 x-ray crystal structures of protein–ligand complexes encompassing 9,117 protein families and 16,044 unique ligands.
• Experimental affinities: Provides binding affinity values (Ka, Kd, Ki, IC50) extracted from primary literature.
• Polypharmacology annotations: Supplies sequence, binding-site, and ligand similarity information to support polypharmacology investigations.
• Pairwise similarity computation: Enables computation of pairwise ligand and binding-site similarities to identify potential polypharmacology pairs.
• Visualization and search integrations: Integrates the NGL viewer for visualization of protein–ligand interactions and implements MarvinJS for small-molecule searching, replacing MarvinView.
• Dataset growth: Expanded by approximately 7,000 new structures (nearly 21% growth) in the latest update.

Scientific Applications:

• Drug repurposing: Use similarity relationships among ligands and binding sites to propose new therapeutic targets for existing compounds.
• Polypharmacology studies: Identify and analyze potential multi-target interactions by comparing sequence, binding-site, and ligand similarities.
• Target prioritization: Leverage structural and affinity data to prioritize protein targets based on ligand-binding similarity profiles.

Methodology:

Data are derived from x-ray crystal structures and binding affinities extracted from primary literature; the resource provides sequence, binding-site, and ligand similarity annotations and supports computation of pairwise ligand and binding-site similarities.