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4GY5

Crystal structure of the tandem tudor domain and plant homeodomain of UHRF1 with Histone H3K9me3

Summary for 4GY5
Entry DOI10.2210/pdb4gy5/pdb
DescriptorE3 ubiquitin-protein ligase UHRF1, Peptide from Histone H3.3, ZINC ION, ... (4 entities in total)
Functional Keywordshistone binding, ligase
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: Q96T88 P84243
Total number of polymer chains6
Total formula weight115359.35
Authors
Cheng, J.,Yang, Y.,Fang, J.,Xiao, J.,Zhu, T.,Chen, F.,Wang, P.,Xu, Y. (deposition date: 2012-09-05, release date: 2012-11-14, Last modification date: 2023-11-08)
Primary citationCheng, J.,Yang, Y.,Fang, J.,Xiao, J.,Zhu, T.,Chen, F.,Wang, P.,Li, Z.,Yang, H.,Xu, Y.
Structural insight into coordinated recognition of trimethylated histone H3 lysine 9 (H3K9me3) by the plant homeodomain (PHD) and tandem tudor domain (TTD) of UHRF1 (ubiquitin-like, containing PHD and RING finger domains, 1) protein
J.Biol.Chem., 288:1329-1339, 2013
Cited by
PubMed: 23161542
DOI: 10.1074/jbc.M112.415398
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.956 Å)
Structure validation

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