The Protein-Ligand Binding Database (PLBD) is a research resource designed and maintained by Vilnius University. It brings together experimental measurements and structural information on interactions between proteins and small-molecule compounds, supporting scientists who study molecular binding and drug design. The database includes thermodynamic data, such as binding affinities and standard enthalpy changes, alongside kinetic parameters.

These values are treated as intrinsic by accounting for binding-linked protonation effects, helping users relate binding energetics to corresponding X-ray crystal structures. PLBD covers diverse compounds, often connected by shared pharmacophoric groups and studied against related proteins, isozymes, or mutants. Its research focuses primarily on human carbonic anhydrases and heat shock proteins.

Users can explore the database scheme, table lists, and descriptions, and consult guidance on citing the resource. PLBD is intended as a platform where researchers can find and contribute thermodynamic, kinetic, and structural data. By placing binding parameters alongside co-crystal structures, it aims to assist the in silico design of new compounds for therapeutic applications