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
Kinases337
Structures (# PDBs)7344
Monomers14826
Unique ligands4453
KLIFS users in Sep-20265898
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News:

Website update and bugfixes

25-Oct-2026

KLIFS @ RSC symposium on kinase inhibitor design

01-May-2023

2023 - a sneak peek

05-Jan-2023
News archive
Latest structures:
PDBKinaseGroupLigand
21oaMAP2K2STEN-{3,4-difluoro-2-[(2-fluoro-4-iodophenyl)amino]-6-methoxyphenyl}-1-[(2S)-2,3-dihydroxypropyl]cyclopropanesulfonamide
21paMAP2K2STEPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
9pwiEGFRTKN-[2-({1-methyl-7-[4-(4-methylpiperazin-1-yl)anilino]-2-oxo-1,4-dihydropyrimido[4,5-d]pyrimidin-3(2H)-yl}methyl)phenyl]prop-2-enamide
9yu9ABL1TK(1S,2S)-N-[2-(4,6-dimethoxypyrimidin-5-yl)-1-methyl-1H-pyrrolo[2,3-c]pyridin-5-yl]-2-fluorocyclopropane-1-carboxamide
9yubABL1TK(1S,2S)-N-[2-(4,6-dimethoxypyrimidin-5-yl)-1-methyl-1H-pyrrolo[2,3-c]pyridin-5-yl]-2-fluorocyclopropane-1-carboxamide