KLIFS, intially developed at the Vrije Universiteit Amsterdam, 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 of 85 residues allows for the comparison of the interaction patterns of kinase-inhibitors to each other to, for example, identify crucial interactions determining kinase-inhibitor selectivity.

For more information you can follow the tutorial, 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
Kinases310
Structures (# PDBs)5456
Monomers11861
Unique ligands3432
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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
7ccuDAPK1CAMKRESVERATROL
7ccvDAPK1CAMKPICEATANNOL
7ccwDAPK1CAMKRESVERATROL
7jy4ALKTK1-{(1S,2S)-1-(2,4-difluorophenyl)-2-[2-(3-methyl-1H-pyrazol-5-yl)-4-(trifluoromethyl)phenoxy]cyclopropyl}methanamine
7jyrALKTK4-{[(1R,2R)-2-(2,4-difluorophenyl)cyclopropyl]oxy}-3-(5-methyl-1H-pyrazol-3-yl)benzonitrile
7jysALKTK3-(3-chlorophenyl)-5-methyl-1H-pyrazole
7jytALKTK3-(3-methyl-1H-pyrazol-5-yl)pyridine