Crystal Structures and Binding Modes of Target Protein-Small Molecule Inhibitor Complexes

This dataset presents high-resolution crystal structures of complexes formed by target proteins (e.g., NF-κB pathway-related proteins, kinases) and small-molecule inhibitors. Using structural biology approaches (e.g., X-ray diffraction), we resolved the spatial conformation of inhibitors in the protein binding pockets, and identified key intermolecular interactions (e.g., hydrogen bonds, hydrophobic interactions) between amino acid residues and inhibitors. These structural data provide core support for target-based drug design, inhibitor optimization, and molecular mechanism studies.