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- PDB-3hsv: Structures of SPOP-Substrate Complexes: Insights into Molecular A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3hsv | ||||||
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Title | Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-MacroH2ASBCpep2 | ||||||
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![]() | protein binding / ligase / ubiquitin / E3 / SPOP / MacroH2A / Nucleus / Ubl conjugation pathway / Alternative splicing / Chromatin regulator / Chromosomal protein / DNA-binding / Isopeptide bond / Methylation / Nucleosome core / Phosphoprotein / Ubl conjugation | ||||||
Function / homology | ![]() negative regulation of cell cycle G2/M phase transition / negative regulation of protein localization to chromosome, telomeric region / regulation of NAD metabolic process / positive regulation of response to oxidative stress / positive regulation of maintenance of mitotic sister chromatid cohesion / regulation of response to oxidative stress / ADP-D-ribose binding / ADP-D-ribose modification-dependent protein binding / negative regulation of transcription of nucleolar large rRNA by RNA polymerase I / sex chromatin ...negative regulation of cell cycle G2/M phase transition / negative regulation of protein localization to chromosome, telomeric region / regulation of NAD metabolic process / positive regulation of response to oxidative stress / positive regulation of maintenance of mitotic sister chromatid cohesion / regulation of response to oxidative stress / ADP-D-ribose binding / ADP-D-ribose modification-dependent protein binding / negative regulation of transcription of nucleolar large rRNA by RNA polymerase I / sex chromatin / sex-chromosome dosage compensation / establishment of protein localization to chromatin / positive regulation of endodermal cell differentiation / double-stranded methylated DNA binding / Barr body / rDNA binding / negative regulation of protein serine/threonine kinase activity / regulation of oxidative phosphorylation / regulation of proteolysis / positive regulation of keratinocyte differentiation / protein serine/threonine kinase inhibitor activity / poly-ADP-D-ribose modification-dependent protein binding / negative regulation of response to oxidative stress / negative regulation of gene expression, epigenetic / Cul3-RING ubiquitin ligase complex / nuclear chromosome / molecular function inhibitor activity / site of DNA damage / regulation of lipid metabolic process / localization / pericentric heterochromatin / heterochromatin organization / epigenetic regulation of gene expression / condensed chromosome / nucleosomal DNA binding / transcription initiation-coupled chromatin remodeling / promoter-specific chromatin binding / RNA polymerase II transcription regulatory region sequence-specific DNA binding / Hedgehog 'on' state / chromatin DNA binding / protein polyubiquitination / structural constituent of chromatin / nucleosome / nucleosome assembly / proteasome-mediated ubiquitin-dependent protein catabolic process / chromosome, telomeric region / transcription cis-regulatory region binding / nuclear speck / protein heterodimerization activity / DNA repair / ubiquitin protein ligase binding / chromatin / nucleolus / protein kinase binding / enzyme binding / negative regulation of transcription by RNA polymerase II / DNA binding / extracellular exosome / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zhuang, M. / Schulman, B.A. / Miller, D. | ||||||
![]() | ![]() Title: Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Authors: Zhuang, M. / Calabrese, M.F. / Liu, J. / Waddell, M.B. / Nourse, A. / Hammel, M. / Miller, D.J. / Walden, H. / Duda, D.M. / Seyedin, S.N. / Hoggard, T. / Harper, J.W. / White, K.P. / Schulman, B.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 144.3 KB | Display | ![]() |
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PDB format | ![]() | 111.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 465.3 KB | Display | ![]() |
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Full document | ![]() | 466.8 KB | Display | |
Data in XML | ![]() | 17.5 KB | Display | |
Data in CIF | ![]() | 25.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3hqhC ![]() 3hqiC ![]() 3hqlC ![]() 3hqmC ![]() 3htmC ![]() 3hu6C ![]() 3hveC ![]() 3ivqC ![]() 3ivvC ![]() 2cr2S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 16485.932 Da / Num. of mol.: 2 / Mutation: D140G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | | Mass: 1536.594 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | #4: Chemical | ChemComp-SO4 / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.55 % |
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.43→50 Å / Num. obs: 54191 / Observed criterion σ(F): 0 / Redundancy: 4.3 % / Rsym value: 0.057 / Net I/σ(I): 31.7 |
Reflection shell | Resolution: 1.43→1.48 Å / Redundancy: 4.2 % / Mean I/σ(I) obs: 14.8 / Num. unique all: 5266 / Rsym value: 0.11 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2CR2 Resolution: 1.43→31.23 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.941 / SU B: 1.875 / SU ML: 0.035 / Cross valid method: THROUGHOUT / ESU R: 0.082 / ESU R Free: 0.07 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 10.51 Å2
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Refinement step | Cycle: LAST / Resolution: 1.43→31.23 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.43→1.468 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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