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Yorodumi- PDB-3qjn: Structural flexibility of Shank PDZ domain is important for its b... -
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-Basic information
Entry | Database: PDB / ID: 3qjn | ||||||
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Title | Structural flexibility of Shank PDZ domain is important for its binding to different ligands | ||||||
Components |
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Keywords | PROTEIN BINDING / PDZ domain / Protein-protein interaction / Beta-PIX | ||||||
Function / homology | Function and homology information presynaptic actin cytoskeleton organization / somatostatin receptor binding / determination of affect / negative regulation of microtubule nucleation / Ephrin signaling / RHOU GTPase cycle / RHOV GTPase cycle / NRAGE signals death through JNK / EGFR downregulation / G alpha (12/13) signalling events ...presynaptic actin cytoskeleton organization / somatostatin receptor binding / determination of affect / negative regulation of microtubule nucleation / Ephrin signaling / RHOU GTPase cycle / RHOV GTPase cycle / NRAGE signals death through JNK / EGFR downregulation / G alpha (12/13) signalling events / RHOQ GTPase cycle / RAC1 GTPase cycle / synaptic receptor adaptor activity / RHOA GTPase cycle / olfactory behavior / synapse maturation / Neurexins and neuroligins / negative regulation of actin filament bundle assembly / storage vacuole / astrocyte cell migration / positive regulation of growth hormone secretion / structural constituent of postsynaptic density / righting reflex / postsynaptic actin cytoskeleton organization / protein localization to synapse / vocalization behavior / habituation / regulation of AMPA receptor activity / ankyrin repeat binding / dendritic spine morphogenesis / gamma-tubulin binding / positive regulation of dendritic spine development / lamellipodium assembly / adult behavior / small GTPase-mediated signal transduction / mitotic spindle pole / Golgi organization / social behavior / positive regulation of excitatory postsynaptic potential / associative learning / neuromuscular process controlling balance / Rho protein signal transduction / excitatory synapse / GABA-ergic synapse / long-term memory / hematopoietic progenitor cell differentiation / ruffle / ionotropic glutamate receptor binding / guanyl-nucleotide exchange factor activity / G protein-coupled receptor binding / modulation of chemical synaptic transmission / Schaffer collateral - CA1 synapse / SH3 domain binding / signaling receptor complex adaptor activity / lamellipodium / cell cortex / growth cone / postsynaptic membrane / postsynapse / scaffold protein binding / protein-containing complex assembly / dendritic spine / postsynaptic density / neuron projection / positive regulation of apoptotic process / focal adhesion / centrosome / dendrite / neuronal cell body / glutamatergic synapse / synapse / protein-containing complex binding / protein kinase binding / protein-containing complex / membrane / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.71 Å | ||||||
Authors | Lee, J.H. / Park, H. / Park, S.J. / Kim, H.J. / Eom, S.H. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2011 Title: The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands Authors: Lee, J.H. / Park, H. / Park, S.J. / Kim, H.J. / Eom, S.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3qjn.cif.gz | 189 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3qjn.ent.gz | 152.9 KB | Display | PDB format |
PDBx/mmJSON format | 3qjn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qj/3qjn ftp://data.pdbj.org/pub/pdb/validation_reports/qj/3qjn | HTTPS FTP |
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-Related structure data
-Links
-Assembly
-Components
#1: Protein | Mass: 12755.696 Da / Num. of mol.: 8 / Fragment: PDZ domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Shank1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9WV48 #2: Protein/peptide | Mass: 847.869 Da / Num. of mol.: 8 / Source method: obtained synthetically / Details: synthetic peptide / References: UniProt: O55043*PLUS #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.19 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100mM MES, 12% ethanol, 10% ethylene glycol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 4A / Wavelength: 1 Å |
Detector | 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: 2.7→30 Å / Num. all: 24385 / Num. obs: 24385 / % possible obs: 94 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 71.03 Å2 |
Reflection shell | Resolution: 2.7→2.8 Å / % possible all: 89.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.71→21.3 Å / Cor.coef. Fo:Fc: 0.8992 / Cor.coef. Fo:Fc free: 0.8467 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso max: 158.44 Å2 / Biso mean: 69.24 Å2 / Biso min: 19.89 Å2
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Refine analyze | Luzzati coordinate error obs: 0.379 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.71→21.3 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.71→2.83 Å / Total num. of bins used: 12
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Refinement TLS params. | Method: refined / Origin x: 35.8438 Å / Origin y: 94.4871 Å / Origin z: 93.7995 Å
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Refinement TLS group | Selection details: { A|656 - A|757 } |