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
Kinases311
Structures (# PDBs)5803
Monomers12536
Unique ligands3630
KLIFS users in Sep-20211291
Your browser unfortunately does not support an HTML5 canvas. Your browser unfortunately does not support an HTML5 canvas.
News:

Powerful analyses using KLIFS data in KNIME

17-Aug-2021

Modified residues and many more clinical candidates

09-Jul-2021

Granular control over the kinase conformation

03-May-2021
News archive
Latest structures:
PDBKinaseGroupLigand
7dxlMERTKTK3-[4-[6-chloranyl-5-[[(3R)-pyrrolidin-3-yl]amino]-1H-indazol-3-yl]pyrazol-1-yl]benzenecarbonitrile
7vkmNTRK1TK-
7vknNTRK1TKRepotrectinib
7vkoNTRK1TKRepotrectinib