2V1D

Structural basis of LSD1-CoREST selectivity in histone H3 recognition

Summary for 2V1D

Related2X0L 2UXX 2IW5 2UXN 2COM 2H94
DescriptorLYSINE-SPECIFIC HISTONE DEMETHYLASE 1, REST COREPRESSOR 1, HISTONE H3.1T, ... (4 entities in total)
Functional Keywordsoxidoreductase repressor complex, alternative splicing, oxidoreductase, flavin, repressor, transcription regulation, chromatin remodelling, host-virus interaction, nuclear protein, phosphorylation, chromatin regulator, oxidoreductase-repressor complex, oxidoreductase/repressor
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationNucleus O60341 Q9UKL0 Q16695
Total number of polymer chains3
Total molecular weight104573.48
Authors
Forneris, F.,Binda, C.,Adamo, A.,Battaglioli, E.,Mattevi, A. (deposition date: 2007-05-23, release date: 2007-05-29, Last modification date: 2011-07-13)
Primary citation
Forneris, F.,Binda, C.,Adamo, A.,Battaglioli, E.,Mattevi, A.
Structural Basis of Lsd1-Corest Selectivity in Histone H3 Recognition.
J.Biol.Chem., 282:20070-, 2007
PubMed: 17537733 (PDB entries with the same primary citation)
DOI: 10.1074/JBC.C700100200
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3.1 Å)
NMR Information
?

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.231183.2%10.4%0.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report