9SXJ

Crystal structure of wild-type c-MET bound by capmatinib.

This is a non-PDB format compatible entry.

Summary for 9SXJ

• Entry DOI: 10.2210/pdb9sxj/pdb
• Descriptor: Hepatocyte growth factor receptor, Capmatinib, DODECAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: kinase, c-met, drug discovery, cancer, nsclc, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 34430.93

Authors

Collie, G.W.,Russell, I.C. (deposition date: 2025-10-09, release date: 2026-02-18, Last modification date: 2026-04-01)

Primary citation

Russell, I.C.,Bachurska-Szpala, P.,van Beek, L.,Michaelides, I.N.,Phillips, C.,Snijder, A.,Stubbs, C.J.,Collie, G.W.
Molecular Basis of c‐MET Inhibition by Approved Small Molecule Drugs: A Structural Perspective.
Acs Med.Chem.Lett., 17:590-597, 2026

PubMed Abstract: The c-MET kinase is a driver of many cancers, and as such, there are a number of small molecule inhibitors of this kinase approved for clinical use. In this Microperspective, we provide a structural overview of the molecular basis by which these drugs inhibit c-MET, focusing on key features contributing to activity, selectivity, and drug resistance. Where necessary, relevant crystal structures not publicly available were determined and are discussed here alongside existing structural data.

PubMed: 41847658
DOI: 10.1021/acsmedchemlett.5c00713

Experimental method

X-RAY DIFFRACTION (1.315 Å)