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- PDB-3hqh: 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: 3hqh | ||||||
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Title | Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx-MacroH2ASBCpep1 | ||||||
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![]() | LIGASE / ubiquitin / SPOP / BTB / E3 / Nucleus / Ubl conjugation pathway | ||||||
Function / homology | ![]() Hedgehog 'on' state / 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 ...Hedgehog 'on' state / 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 / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / chromosome, telomeric region / transcription cis-regulatory region binding / protein ubiquitination / 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. | ||||||
![]() | ![]() 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 | ![]() | 43.5 KB | Display | ![]() |
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PDB format | ![]() | 29.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.9 KB | Display | ![]() |
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Full document | ![]() | 438.9 KB | Display | |
Data in XML | ![]() | 8.2 KB | Display | |
Data in CIF | ![]() | 10.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3hqiC ![]() 3hqlC ![]() 3hqmC ![]() 3hsvC ![]() 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
#1: Protein | Mass: 16485.932 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Protein/peptide | Mass: 1422.429 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide / References: UniProt: O75367*PLUS | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.82 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 12% PEG550, 0.1M MES 6.5, 20mM ZnSO4 , VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-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: 2.29→50 Å / Num. all: 8052 / Num. obs: 8052 / Observed criterion σ(F): 0 / Observed criterion σ(I): 8.3 / Redundancy: 7 % / Rmerge(I) obs: 0.09 / Rsym value: 0.09 / Net I/σ(I): 31.7 |
Reflection shell | Resolution: 2.29→2.37 Å / Redundancy: 4.5 % / Mean I/σ(I) obs: 8.3 / Rsym value: 0.182 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2cr2.pdb Resolution: 2.3→50 Å / Cross valid method: Rfree / σ(F): 0 / σ(I): 8.3
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Refinement step | Cycle: LAST / Resolution: 2.3→50 Å
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