PLIP: fully automated protein–ligand interaction profiler

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ID: 291070
2015
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Abstract
The characterization of interactions in protein-ligand complexes is essential for research in structural bioinformatics, drug discovery and biology.However, comprehensive tools are not freely available to the research community.Here, we present the protein-ligand interaction profiler (PLIP), a novel web service for fully automated detection and visualization of relevant non-covalent proteinligand contacts in 3D structures, freely available at projects.biotec.tu-dresden.de/plip-web.The input is either a Protein Data Bank structure, a protein or ligand name, or a custom protein-ligand complex (e.g. from docking).In contrast to other tools, the rule-based PLIP algorithm does not require any structure preparation.It returns a list of detected interactions on single atom level, covering seven interaction types (hydrogen bonds, hydrophobic contacts, pi-stacking, pi-cation interactions, salt bridges, water bridges and halogen bonds).PLIP stands out by offering publication-ready images, PyMOL session files to generate custom images and parsable result files to facilitate successive data processing.The full python source code is available for download on the website.PLIP's command-line mode allows for high-throughput interaction profiling.
Reference Key
openalex_W2025816743 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Sebastian Salentin, Sven B. Schreiber, V. Joachim Haupt, Melissa F. Adasme, Michael Schroeder
Journal Nucleic Acids Research
Year 2015
DOI
10.1093/nar/gkv315
URL
https://doi.org/10.1093/nar/gkv315
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