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Structure paper

TitleComprehensive characterization of EGFR-tyrosine kinase inhibitor interactions probed by hydrogen-deuterium exchange and mass spectrometry (HDX-MS)
Journal, issue, pagesTo Be Published
Publish dateMay 23, 2024 (structure data deposition date)
AuthorsTsutsui, Y. / Ashtekar, K.D. / Stayrook, S. / Lemmon, M.A.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.307 - 2.551 Å
Structure data

PDB-9by4:
Co-crystal structure of the kinase domain of EGFR with non-covalent osimertinib
Method: X-RAY DIFFRACTION / Resolution: 2.307 Å

PDB-9by6:
Crystal structure of the kinase domain of EGFR soaked with non-covalent osimertinib
Method: X-RAY DIFFRACTION / Resolution: 2.551 Å

Chemicals

ChemComp-PDO:
1,3-PROPANDIOL

ChemComp-Q6K:
~{N}-[2-[2-(dimethylamino)ethyl-methyl-amino]-4-methoxy-5-[[4-(1-methylindol-3-yl)pyrimidin-2-yl]amino]phenyl]propanamide

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-YY3:
N-(2-{[2-(dimethylamino)ethyl](methyl)amino}-4-methoxy-5-{[4-(1-methyl-1H-indol-3-yl)pyrimidin-2-yl]amino}phenyl)prop-2-enamide / medication, inhibitor*YM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / EGFR / kinase domain / ONCOPROTEIN

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