2LGK

NMR Structure of UHRF1 PHD domains in a complex with histone H3 peptide

Summary for 2LGK

Related2LGG 2LGL
DescriptorE3 ubiquitin-protein ligase UHRF1, histone H3 peptide, ZINC ION (3 entities in total)
Functional Keywordsuhrf1, phd, histone h3, ligase-dna binding protein complex, ligase/dna binding protein
Biological sourceHomo sapiens
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Cellular locationNucleus Q96T88
Total number of polymer chains2
Total molecular weight9396.69
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)
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 (PDB entries with the same primary citation)
DOI: 10.1038/cr.2011.123
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers261.1%11.0%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures
Download full validation report