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Open data
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Basic information
Entry | Database: PDB / ID: 2n2h | ||||||
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Title | Solution structure of Sds3 in complex with Sin3A | ||||||
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Function / homology | ![]() cellular response to tert-butyl hydroperoxide / Regulation of MECP2 expression and activity / response to methylglyoxal / SUMOylation of transcription cofactors / regulation of hormone levels / HDACs deacetylate histones / cerebral cortex neuron differentiation / blastocyst hatching / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / negative regulation of circadian rhythm ...cellular response to tert-butyl hydroperoxide / Regulation of MECP2 expression and activity / response to methylglyoxal / SUMOylation of transcription cofactors / regulation of hormone levels / HDACs deacetylate histones / cerebral cortex neuron differentiation / blastocyst hatching / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / negative regulation of circadian rhythm / Regulation of lipid metabolism by PPARalpha / Cytoprotection by HMOX1 / negative regulation of stem cell population maintenance / Ub-specific processing proteases / cellular response to dopamine / transcription regulator inhibitor activity / negative regulation of protein localization to nucleus / regulation of axon extension / positive regulation of stem cell population maintenance / Sin3-type complex / type I interferon-mediated signaling pathway / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Clark, M. / Radhakrishnan, I. | ||||||
![]() | ![]() Title: Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex. Authors: Clark, M.D. / Marcum, R. / Graveline, R. / Chan, C.W. / Xie, T. / Chen, Z. / Ding, Y. / Zhang, Y. / Mondragon, A. / David, G. / Radhakrishnan, I. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 975.5 KB | Display | ![]() |
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PDB format | ![]() | 819 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 3125.531 Da / Num. of mol.: 1 / Fragment: UNP residues 205-228 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 14698.822 Da / Num. of mol.: 1 / Fragment: UNP residues 608-729 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 0.12 / pH: 6.7 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Agilent DD2 / Manufacturer: Agilent / Model![]() |
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Processing
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Refinement | Method: ![]() | |||||||||
NMR representative | Selection criteria: closest to the average | |||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 80 / Conformers submitted total number: 20 |