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
Kinases314
Structures (# PDBs)6003
Monomers12823
Unique ligands3753
KLIFS users in May-20221915
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News:

KLIFS workshop @ May 19th

02-Apr-2022

Alternative coloring scheme

01-Feb-2022

Five "hidden" KLIFS features

23-Dec-2021
News archive
Latest structures:
PDBKinaseGroupLigand
7b55Camk2aCAMK-
7b56Camk2aCAMK-
7b57Camk2aCAMK-
7f2xMAP2K1STEPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
7n8tMAPK9CMGCADENOSINE MONOPHOSPHATE
7oteSRCTK3-(imidazo[1,2-b]pyridazin-3-ylethynyl)-4-methyl-N-{4-[(4-methylpiperazin-1-yl)methyl]-3-(trifluoromethyl)phenyl}benzamide