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TitleCrystal structures of histone and p53 methyltransferase SmyD2 reveal a conformational flexibility of the autoinhibitory C-terminal domain.
Journal, issue, pagesPlos One, Vol. 6, Page e21640-e21640, Year 2011
Publish dateFeb 28, 2011 (structure data deposition date)
AuthorsJiang, Y. / Sirinupong, N. / Brunzelle, J. / Yang, Z.
External linksPlos One / PubMed:21738746
MethodsX-ray diffraction
Resolution1.8 - 2.03 Å
Structure data

PDB-3qwv:
Crystal structure of histone lysine methyltransferase SmyD2 in complex with the cofactor product AdoHcy
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

PDB-3qww:
Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SFG:
SINEFUNGIN

Source
  • mus musculus (house mouse)
KeywordsTRANSFERASE / Methyltransferase / Hsp90 / TRANSFERASE/TRANSFERASE INHIBITOR / TRANSFERASE-TRANSFERASE INHIBITOR complex

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