Structures and chemical shift assignments for the ADD domain of the ATRX protein

Summary for 2JM1

DescriptorTranscriptional regulator ATRX, ZINC ION (2 entities in total)
Functional Keywordsadd domain, metal binding protein
Biological sourceHomo sapiens (human)
Cellular locationNucleus P46100
Total number of polymer chains1
Total molecular weight16413.78
Yang, J.,Neuhaus, D. (deposition date: 2006-09-13, release date: 2007-06-26, Last modification date: 2011-07-13)
Primary citation
Argentaro, A.,Yang, J.C.,Chapman, L.,Kowalczyk, M.S.,Gibbons, R.J.,Higgs, D.R.,Neuhaus, D.,Rhodes, D.
Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.
Proc.Natl.Acad.Sci.USA, 104:11939-11944, 2007
PubMed: 17609377 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.0704057104
MImport into Mendeley
Experimental method
NMR Information

Structure validation

ClashscoreRamachandran outliersSidechain outliers253.4%11.9%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures
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