MANORAA is published today!
Tanramluk D, Narupiyakul L, Akavipat R, Gong S, Charoensawan V MANORAA (Mapping Analogous Nuclei Onto Residue And Affinity) for identifying protein-ligand fragment interaction, pathways and SNPs. Nucl. Acids Res. (08 July 2016) 44 (W1): W514-W521.
Protein-ligand interaction analysis is crucial for drug design and protein engineering in order to predict the binding affinity and selectivity of ligands for the target proteins. The MANORAA server, Mapping Analogous Nuclei Onto Residue And Affinity, provides a user-friendly web interface to assist structural study and design of protein-ligand interactions by harvesting information from the PDBe, UniProt, ChemBL, KEGG, OpenTargets, SAMUL and Credo. Our flexible SMILES input panel in conjunction with ligand linked out to various databases allows the user to harvest ligand-oriented information such as pathways, off-target proteins, human variants and target systems. The server can drill down to the chemical interactions made by analogous ligand substructures. Conserved features and differences identified from the server will open doors for a robust and insightful analysis of promiscuity, selectivity and trends in binding affinities of the ligand with various proteins.