Kinase-Ligand Interaction Fingerprints and Structures database (KLIFS), developed at the Division of Medicinal Chemistry - VU University Amsterdam, is a database that revolves around the protein structure of catalytic kinase domains and the way kinase inhibitors can interact with them. Based on the underlying systematic and consistent protocol all (currently human and mouse) kinase structures and the binding mode of kinase ligands can be directly compared to each other. Moreover, because of the classification of an all-encompassing binding site of 85 residues it is possible to compare the interaction patterns of kinase-inhibitors to each other to, for example, identify crucial interactions determining kinase-inhibitor selectivity.

Follow the tutorial, read our Nucleic Acids Research publication and ACS Journal of Medicinal Chemistry publication, or see the frequently asked questions (FAQ) for more information about the possibilities of KLIFS.

Animation of the stuctural kinome coverage through time here.

News:
01-Aug-2018

Release version 2.4 - the quality and stability release


30-May-2017

Release version 2.3 - the atypical Protein Kinase (aPK) release


News archive

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Contents:
Species: 2
Groups: 9
Families: 98
Kinases: 291
PDB entries: 4452
Monomers: 9342
Unique ligands: 2840

Latest additions:
PDBKinaseFamilyGroupLigand
ROCK1DMPKAGCTo be updated
ROCK2DMPKAGCTo be updated
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