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

Wang, C.,Shen, J.,Yang, Z.,Chen, P.,Zhao, B.,Hu, W.,Lan, W.,Tong, X.,Wu, H.,Li, G.,Cao, C. (deposition date: 2011-07-28, release date: 2011-09-28, Last modification date: 2023-06-14)

• 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; PubMed: 21808299; DOI: 10.1038/cr.2011.123

Experimental method

SOLUTION NMR