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TitleRegulation of p53 activity through lysine methylation
Journal, issue, pagesNature, Vol. 432, Page 353-360, Year 2004
Publish dateOct 12, 2004 (structure data deposition date)
AuthorsChuikov, S. / Kurash, J.K. / Wilson, J.R. / Xiao, B. / Justin, N. / Ivanov, G.S. / McKinney, K. / Tempst, P. / Prives, C. / Gamblin, S.J. ...Chuikov, S. / Kurash, J.K. / Wilson, J.R. / Xiao, B. / Justin, N. / Ivanov, G.S. / McKinney, K. / Tempst, P. / Prives, C. / Gamblin, S.J. / Barlev, N.A. / Reinberg, D.
External linksNature / PubMed:15525938
MethodsX-ray diffraction
Resolution1.75 Å
Structure data

PDB-1xqh:
Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Set9-p53 complex / Set-domain / Lysine methylation

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