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- PDB-3hu6: 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: 3hu6 | ||||||
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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 / ubiquitin / E3 / SPOP / Puckered / Nucleus / Ubl conjugation pathway / Hydrolase | ||||||
Function / homology | ![]() imaginal disc eversion / imaginal disc fusion / RAF-independent MAPK1/3 activation / chorion micropyle formation / embryonic anterior midgut (ectodermal) morphogenesis / imaginal disc fusion, thorax closure / chitin-based embryonic cuticle biosynthetic process / JUN kinase phosphatase activity / imaginal disc-derived male genitalia morphogenesis / determination of digestive tract left/right asymmetry ...imaginal disc eversion / imaginal disc fusion / RAF-independent MAPK1/3 activation / chorion micropyle formation / embryonic anterior midgut (ectodermal) morphogenesis / imaginal disc fusion, thorax closure / chitin-based embryonic cuticle biosynthetic process / JUN kinase phosphatase activity / imaginal disc-derived male genitalia morphogenesis / determination of digestive tract left/right asymmetry / negative regulation of stress-activated protein kinase signaling cascade / Negative regulation of MAPK pathway / negative regulation of peptidoglycan recognition protein signaling pathway / dorsal closure / follicle cell of egg chamber development / MAP kinase tyrosine phosphatase activity / protein tyrosine/threonine phosphatase activity / dorsal appendage formation / compound eye development / positive regulation of border follicle cell migration / MAP kinase tyrosine/serine/threonine phosphatase activity / regulation of proteolysis / negative regulation of programmed cell death / negative regulation of MAPK cascade / myosin phosphatase activity / Cul3-RING ubiquitin ligase complex / molecular function inhibitor activity / protein-serine/threonine phosphatase / phosphoprotein phosphatase activity / protein secretion / negative regulation of tumor necrosis factor-mediated signaling pathway / localization / epidermis development / JNK cascade / regulation of G2/M transition of mitotic cell cycle / protein dephosphorylation / protein-tyrosine-phosphatase / determination of adult lifespan / Hedgehog 'on' state / wound healing / protein polyubiquitination / positive regulation of immune response / cellular response to oxidative stress / actin cytoskeleton organization / proteasome-mediated ubiquitin-dependent protein catabolic process / response to oxidative stress / nuclear speck / ubiquitin protein ligase binding / positive regulation of gene expression / negative regulation of apoptotic process / Golgi apparatus / endoplasmic reticulum / nucleoplasm / nucleus / cytoplasm / cytosol 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 | ![]() | 128.2 KB | Display | ![]() |
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PDB format | ![]() | 99.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 450.8 KB | Display | ![]() |
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Full document | ![]() | 468.3 KB | Display | |
Data in XML | ![]() | 25.8 KB | Display | |
Data in CIF | ![]() | 35.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3hqhSC ![]() 3hqiC ![]() 3hqlC ![]() 3hqmC ![]() 3hsvC ![]() 3htmSC ![]() 3hveC ![]() 3ivqC ![]() 3ivvC 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: 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 / Fragment: UNP residues 96-102 / Source method: obtained synthetically References: UniProt: Q9VHV8, Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases, protein-serine/threonine phosphatase, protein-tyrosine-phosphatase #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.6 % |
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-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 | Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 25440 / Observed criterion σ(F): 0 / Redundancy: 9.4 % / Rsym value: 0.174 / Net I/σ(I): 20.1 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 5.9 % / Mean I/σ(I) obs: 2.4 / Num. unique all: 1877 / Rsym value: 0.59 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entries 3HQH, 3HTM Resolution: 2.7→50 Å / σ(F): 0
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
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