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
Kinases326
Structures (# PDBs)6667
Monomers13852
Unique ligands4148
KLIFS users in Apr-20241735
Your browser unfortunately does not support an HTML5 canvas. Your browser unfortunately does not support an HTML5 canvas.
News:

KLIFS @ RSC symposium on kinase inhibitor design

01-May-2023

2023 - a sneak peek

05-Jan-2023

KLIFS workshop @ May 19th

02-Apr-2022
News archive
Latest structures:
PDBKinaseGroupLigand
8h6ePRPF4BCMGC-
8h6jPRPF4BCMGC-