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3DB3

Crystal structure of the tandem tudor domains of the E3 ubiquitin-protein ligase UHRF1 in complex with trimethylated histone H3-K9 peptide

Summary for 3DB3
Entry DOI10.2210/pdb3db3/pdb
Related2FAZ 3BI7 3CLZ 3DB4
DescriptorE3 ubiquitin-protein ligase UHRF1, Trimethylated histone H3-K9 peptide (3 entities in total)
Functional Keywordscell cycle, dna damage, dna repair, tandem tudor domains, ligase, metal binding, dna replication, transcriptional silencing, chromatin, phosphorylation, transcription, transcription regulation, ubl conjugation pathway, zinc-finger, structural genomics, structural genomics consortium, sgc, dna-binding, metal-binding, nucleus, phosphoprotein
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: Q96T88 Q71DI3
Total number of polymer chains2
Total formula weight19718.38
Authors
Primary citationNady, N.,Lemak, A.,Walker, J.R.,Avvakumov, G.V.,Kareta, M.S.,Achour, M.,Xue, S.,Duan, S.,Allali-Hassani, A.,Zuo, X.,Wang, Y.X.,Bronner, C.,Chedin, F.,Arrowsmith, C.H.,Dhe-Paganon, S.
Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein.
J.Biol.Chem., 286:24300-24311, 2011
Cited by
PubMed: 21489993
DOI: 10.1074/jbc.M111.234104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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