2LGK
NMR Structure of UHRF1 PHD domains in a complex with histone H3 peptide
Summary for 2LGK
Entry DOI | 10.2210/pdb2lgk/pdb |
Related | 2LGG 2LGL |
NMR Information | BMRB: 17812 |
Descriptor | E3 ubiquitin-protein ligase UHRF1, histone H3 peptide, ZINC ION (3 entities in total) |
Functional Keywords | uhrf1, phd, histone h3, ligase-dna binding protein complex, ligase/dna binding protein |
Biological source | Homo sapiens More |
Cellular location | Nucleus: Q96T88 |
Total number of polymer chains | 2 |
Total formula weight | 9396.69 |
Authors | |
Primary citation | Wang, 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: 21808299DOI: 10.1038/cr.2011.123 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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