+Open data
-Basic information
Entry | Database: PDB / ID: 4zqa | |||||||||
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Title | Crystal Structure of the Sds3 Dimerization Domain | |||||||||
Components | Sin3 histone deacetylase corepressor complex component SDS3 | |||||||||
Keywords | TRANSCRIPTION REPRESSOR / transcription repression / histone deacetylase complex / coiled-coil / corepressor complex | |||||||||
Function / homology | Function and homology information HDACs deacetylate histones / blastocyst hatching / negative regulation of stem cell population maintenance / Ub-specific processing proteases / Sin3-type complex / positive regulation of stem cell population maintenance / negative regulation of cell migration / negative regulation of transforming growth factor beta receptor signaling pathway / histone deacetylase binding / nuclear body ...HDACs deacetylate histones / blastocyst hatching / negative regulation of stem cell population maintenance / Ub-specific processing proteases / Sin3-type complex / positive regulation of stem cell population maintenance / negative regulation of cell migration / negative regulation of transforming growth factor beta receptor signaling pathway / histone deacetylase binding / nuclear body / chromatin remodeling / negative regulation of DNA-templated transcription / apoptotic process / negative regulation of transcription by RNA polymerase II / enzyme binding / identical protein binding / nucleus / cytosol Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 1.65 Å | |||||||||
Authors | Chan, C.W. / Mondragon, A. / Clark, M. / Radhakrishnan, I. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2015 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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4zqa.cif.gz | 56 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4zqa.ent.gz | 41.4 KB | Display | PDB format |
PDBx/mmJSON format | 4zqa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zq/4zqa ftp://data.pdbj.org/pub/pdb/validation_reports/zq/4zqa | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 10396.940 Da / Num. of mol.: 1 / Fragment: UNP residues 90-172 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Suds3, Sds3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8BR65 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.26 % |
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Crystal grow | Temperature: 287 K / Method: vapor diffusion, sitting drop / pH: 7.4 Details: 15% ethanol (v/v), 200 mM MgCl2, and 100 mM imidazole PH range: 7.2-7.8 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97856, 0.97872 | |||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 9, 2014 | |||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.65→35.5 Å / Num. obs: 13534 / % possible obs: 94.2 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.045 / Net I/σ(I): 11.3 | |||||||||
Reflection shell | Resolution: 1.65→1.68 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.246 / Mean I/σ(I) obs: 2.8 / Num. unique all: 667 / % possible all: 96.5 |
-Processing
Software |
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Refinement | Method to determine structure: SIRAS / Resolution: 1.65→33 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.956 / SU B: 5.328 / SU ML: 0.076 / Cross valid method: THROUGHOUT / ESU R: 0.114 / ESU R Free: 0.093 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.075 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→33 Å
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Refine LS restraints |
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