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2LGG

Structure of PHD domain of UHRF1 in complex with H3 peptide

Summary for 2LGG
Entry DOI10.2210/pdb2lgg/pdb
Related2LGK 2LGL
NMR InformationBMRB: 17808
DescriptorE3 ubiquitin-protein ligase UHRF1, histone H3 peptide, ZINC ION (3 entities in total)
Functional Keywordsdna binding protein/gene regulation, ligase-dna binding protein complex, ligase/dna binding protein
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: Q96T88
Total number of polymer chains2
Total formula weight9354.61
Authors
Wang, C.,Shen, J.,Yang, Z.,Chen, P.,Zhao, B.,Hu, W.,Lan, W.,Tong, X.,Wu, H.,Li, G.,Cao, C. (deposition date: 2011-07-26, release date: 2011-09-28, Last modification date: 2023-06-14)
Primary citationWang, C.,Shen, J.,Yang, Z.,Chen, P.,Zhao, B.,Hu, W.,Lan, W.,Tong, X.,Wu, H.,Li, G.,Cao, C.
Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger.
Cell Res., 21:1379-1382, 2011
Cited by
PubMed: 21808299
DOI: 10.1038/cr.2011.123
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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