KLIFS, intially developed at the Vrije Universiteit Amsterdam, is a 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)5337
Monomers11620
Unique ligands3363
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News:

KLIFS v3 in Nucleic Acids Research

21-Oct-2020

Release version 3.0 - the overhaul release

09-Sep-2020

Trends in Pharmacological Sciences publication (open access)

31-Oct-2019
News archive
Latest structures:
PDBKinaseGroupLigand
6seqLMTK3TK-
6x8gTYK2TKtrans-3-(cyanomethyl)-3-{4-[6-(1-methyl-1H-pyrazol-4-yl)pyrazolo[1,5-a]pyrazin-4-yl]-1H-pyrazol-1-yl}cyclobutane-1-carbonitrile
7c2vIRAK4TKL2-(2-methylpyridin-4-yl)-N-[2-morpholin-4-yl-5-[(3R)-3-oxidanylpyrrolidin-1-yl]-[1,3]oxazolo[4,5-b]pyridin-6-yl]-1,3-oxazole-4-carboxamide
7c2wIRAK4TKL-