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TitleStructural basis for the product specificity of histone lysine methyltransferases
Journal, issue, pagesMol. Cell, Vol. 12, Page 177-185, Year 2003
Publish dateMay 21, 2003 (structure data deposition date)
AuthorsZhang, X. / Yang, Z. / Khan, S.I. / Horton, J.R. / Tamaru, H. / Selker, E.U. / Cheng, X.
External linksMol. Cell / PubMed:12887903
MethodsX-ray diffraction
Resolution2.59 Å
Structure data

PDB-1peg:
Structural basis for the product specificity of histone lysine methyltransferases
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • neurospora crassa (fungus)
KeywordsTRANSFERASE / Ternary structure of DIM-5 / a SUV39-type histone-H3 Lys-9 methyltransferase / SET domain protein forms a knot-like substructure / pre-SET triangular Zn3Cys9 zinc cluster / post-SET zinc-binding site / a hybrid beta sheet formed by DIM-5 and H3 tail

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