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3ASK

Structure of UHRF1 in complex with histone tail

Summary for 3ASK
Entry DOI10.2210/pdb3ask/pdb
Related2FAZ 2ZKD 2ZO0 3ASL 3CLZ 3DB3 3FL2
DescriptorE3 ubiquitin-protein ligase UHRF1, Histone H3.3, ZINC ION, ... (4 entities in total)
Functional Keywordshistone reader modules, epigenetic regulation, histone h3, trimethylaion of lysine residue, ligase-dna binding protein complex, ligase/dna binding protein
Biological sourceHomo sapiens (human)
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Cellular locationNucleus: Q96T88 P84243
Total number of polymer chains7
Total formula weight109495.07
Authors
Arita, K.,Sugita, K.,Unoki, M.,Hamamoto, R.,Sekiyama, N.,Tochio, H.,Ariyoshi, M.,Shirakawa, M. (deposition date: 2010-12-16, release date: 2012-01-25, Last modification date: 2013-06-05)
Primary citationArita, K.,Isogai, S.,Oda, T.,Unoki, M.,Sugita, K.,Sekiyama, N.,Kuwata, K.,Hamamoto, R.,Tochio, H.,Sato, M.,Ariyoshi, M.,Shirakawa, M.
Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1
Proc.Natl.Acad.Sci.USA, 109:12950-12955, 2012
Cited by
PubMed: 22837395
DOI: 10.1073/pnas.1203701109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.904 Å)
Structure validation

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