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Structure paper

TitleStructural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding.
Journal, issue, pagesNucleic Acids Res., Vol. 39, Page 4438-4449, Year 2011
Publish dateSep 21, 2010 (structure data deposition date)
AuthorsXu, S. / Wu, J. / Sun, B. / Zhong, C. / Ding, J.
External linksNucleic Acids Res. / PubMed:21266482
MethodsX-ray diffraction
Resolution2.82 - 3.6 Å
Structure data

PDB-3oxf:
Human lysine methyltransferase Smyd3 in complex with AdoHcy (Form I)
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

PDB-3oxg:
human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III)
Method: X-RAY DIFFRACTION / Resolution: 3.41 Å

PDB-3oxl:
Human lysine methyltransferase Smyd3 in complex with AdoHcy (Form II)
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

Chemicals

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Smyd proteins / MYND / SET domain / histone lysine methyltransferase / histone methylation / H3K4

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