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3F9Z

Structural Insights into Lysine Multiple Methylation by SET Domain Methyltransferases, SET8-Y245F / H4-Lys20 / AdoHcy

Summary for 3F9Z
Entry DOI10.2210/pdb3f9z/pdb
Related1ZKK 3F9W 3F9X 3F9Y
DescriptorHistone-lysine N-methyltransferase SETD8, Histone H4, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
Functional Keywordsmethyltransferase, histone, set, lysine, alternative splicing, cell cycle, cell division, chromatin regulator, chromosomal protein, coiled coil, mitosis, nucleus, repressor, s-adenosyl-l-methionine, transcription, transcription regulation, acetylation, dna-binding, methylation, nucleosome core, transferase
Biological sourceHomo sapiens
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Cellular locationNucleus: Q9NQR1 P62805
Total number of polymer chains8
Total formula weight81772.90
Authors
Couture, J.-F.,Dirk, L.M.A.,Brunzelle, J.S.,Houtz, R.L.,Trievel, R.C. (deposition date: 2008-11-14, release date: 2008-11-25, Last modification date: 2023-09-06)
Primary citationCouture, J.F.,Dirk, L.M.,Brunzelle, J.S.,Houtz, R.L.,Trievel, R.C.
Structural origins for the product specificity of SET domain protein methyltransferases.
Proc.Natl.Acad.Sci.Usa, 105:20659-20664, 2008
Cited by
PubMed: 19088188
DOI: 10.1073/pnas.0806712105
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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