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TitleAllosteric Inhibition of PKMYT1 Induces a Unique, Inactive ATP Binding Site Conformation.
Journal, issue, pagesJ. Am. Chem. Soc., Year 2026
Publish dateMay 13, 2026 (structure data deposition date)
AuthorsHerrington, N.B. / Khamrui, S. / Zhao, Y. / Lansiquot, C. / Wu, R. / Pandey, G. / Lazarus, M.B. / Schlessinger, A.
External linksJ. Am. Chem. Soc. / PubMed:42227652
MethodsX-ray diffraction
Resolution1.95 - 2.22 Å
Structure data

PDB-13lv:
Structure of PKMYT1 bound to allosteric inhibitor P29-(S)
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

PDB-13lw:
Structure of PKMYT1 bound to inhibitor P32-(S)
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-13lx:
Structure of PKMYT1 bound to inhibitor P32-(R)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

PDB-1dg4:
NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM

ChemComp-HOH:
WATER

PDB-1dg6:
CRYSTAL STRUCTURE OF APO2L/TRAIL

PDB-1dg5:
DIHYDROFOLATE REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND TRIMETHOPRIM

Source
  • homo sapiens (human)
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / kinase / PKMYT1 / inhibitor / allosteric / TRANSFERASE / TRANSFERASE-TRANSFERASE INHIBITOR complex

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