KLIFS is a kinase database that dissects experimental structures of catalytic kinase domains and the way kinase inhibitors interact with them. The KLIFS structural alignment enables the comparison of all structures and ligands to each other. Moreover, the KLIFS residue numbering scheme capturing the catalytic cleft with 85 residues enables the comparison of the interaction patterns of kinase-inhibitors, for example, to identify crucial interactions determining kinase-inhibitor selectivity.

For more information, go through the frequently asked questions (FAQ) or read our articles in Nucleic Acids Research (2020), Trends in Pharmacological Sciences (2019), and ACS Journal of Medicinal Chemistry (2014).

Statistics
Kinases312
Structures (# PDBs)5553
Monomers12122
Unique ligands3491
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News:

KLIFS presentation @ February 10th

15-Jan-2021

KLIFS v3 in Nucleic Acids Research

21-Oct-2020

Release version 3.0 - the overhaul release

09-Sep-2020
News archive
Latest structures:
PDBKinaseGroupLigand
7akmCHEK1CAMKPHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
7akmCHEK1CAMK-
7akoCHEK1CAMKSTAUROSPORINE
7ax4TYK2-bTK2-(carbamoylamino)-5-(4-fluorophenyl)thiophene-3-carboxamide
7bw7INSRTK-
7bw8INSRTK-
7e34CDK2CMGC-
7lt3ANTXR1AtypicalADENOSINE-5'-DIPHOSPHATE