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.


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


Publication and release 3D-e-Chem-VM

News archive

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Species: 2
Groups: 9
Families: 97
Kinases: 288
PDB entries: 4293
Monomers: 8921
Unique ligands: 2738

Latest additions:
MAPK7MAPKCMGCTo be updated
MAP4K4STE20STETo be updated
PTK6SrcTKTo be updated
PTK6SrcTKTo be updated
Pik3cdPIKAtypicalTo be updated
GSK3BGSKCMGCTo be updated
PIK3CGPIKAtypicalTo be updated
CSNK1G3CK1CK1To be updated
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