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- PDB-3hqi: 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: 3hqi | ||||||
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Title | Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases: SPOPMATHx/BTB/3-box-PucSBC1 | ||||||
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![]() | PROTEIN BINDING / Ligase / SPOP / E3 / Ubiquitin / Puckered / Nucleus / Ubl conjugation pathway | ||||||
Function / homology | ![]() regulation of proteolysis / Cul3-RING ubiquitin ligase complex / molecular function inhibitor activity / localization / Hedgehog 'on' state / protein polyubiquitination / proteasome-mediated ubiquitin-dependent protein catabolic process / nuclear speck / ubiquitin protein ligase binding / nucleoplasm ...regulation of proteolysis / Cul3-RING ubiquitin ligase complex / molecular function inhibitor activity / localization / Hedgehog 'on' state / protein polyubiquitination / proteasome-mediated ubiquitin-dependent protein catabolic process / nuclear speck / ubiquitin protein ligase binding / 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 | ![]() | 125.8 KB | Display | ![]() |
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PDB format | ![]() | 98.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.2 KB | Display | ![]() |
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Full document | ![]() | 463.1 KB | Display | |
Data in XML | ![]() | 23.3 KB | Display | |
Data in CIF | ![]() | 31.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3hqhSC ![]() 3hqlC ![]() 3hqmC ![]() 3hsvC ![]() 3htmC ![]() 3hu6C ![]() 3hveC ![]() 3ivqC ![]() 3ivvC S: Starting model for refinement C: citing same article ( |
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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: 35228.309 Da / Num. of mol.: 2 / Fragment: UNP residues 28-329 / Mutation: D140G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 751.737 Da / Num. of mol.: 2 / Source method: obtained synthetically #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.58 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.5 / Details: pH 5.5, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Date: Jul 31, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.62→50 Å / Num. all: 24800 / Num. obs: 24800 / Observed criterion σ(F): 0 / Redundancy: 4.6 % / Rsym value: 0.106 / Net I/σ(I): 20 |
Reflection shell | Resolution: 2.62→2.71 Å / Redundancy: 3.8 % / Mean I/σ(I) obs: 3.7 / Num. unique all: 2213 / Rsym value: 0.296 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3HQH Resolution: 2.62→50 Å / σ(F): 0 / σ(I): 3.7
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.62→50 Å
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