Protein-Ligand Binding Database

Designed and maintained by Vilnius University


The PLBD contains thermodynamic and kinetic data describing protein‑small molecule compound (ligand) interactions. Thermodynamic parameters include not only the affinities, but also the changes in standard enthalpies of binding. The thermodynamic and kinetic parameters are intrinsic, where binding‑linked protonation of compound and protein were subtracted to enable the correlation of binding energies with the X‑ray crystallographic structures whose PDB list is provided. The interacting compounds are diverse but often related via a pharmacophoric group that governs the interaction with a series of highly related proteins, isozymes or mutants. Here we study primarily the two classes of proteins, human carbonic anhydrases and heat shock proteins.

This database was designed to become a universal platform for scientists to find and deposit thermodynamic, kinetic, and structural parameters of protein‑ligand interaction. The PLBD describes the thermodynamic parameters of binding next to the co‑crystal structures that should help in the in silico design of novel compounds for therapeutic purposes.

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Prof. Daumantas Matulis
Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Lithuania.
journal icon How to cite
LinkuvienÄ— V. et al., 2018. DOI: 10.1017/s0033583518000082