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Yorodumi- PDB-4lnp: The first SH3 domain from CAP/Ponsin in complex with proline rich... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4lnp | ||||||
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Title | The first SH3 domain from CAP/Ponsin in complex with proline rich peptide from Vinculin | ||||||
Components |
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Keywords | SIGNALING PROTEIN / sh3 domain / cell migration / proline rich peptide / focal adhesion | ||||||
Function / homology | Function and homology information regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / cell-substrate junction / terminal web / epithelial cell-cell adhesion / zonula adherens / dystroglycan binding / alpha-catenin binding ...regulation of protein localization to adherens junction / podosome ring / outer dense plaque of desmosome / inner dense plaque of desmosome / cell-substrate junction / terminal web / epithelial cell-cell adhesion / zonula adherens / dystroglycan binding / alpha-catenin binding / flotillin complex / fascia adherens / cell-cell contact zone / costamere / apical junction assembly / regulation of establishment of endothelial barrier / adherens junction assembly / focal adhesion assembly / axon extension / protein localization to cell surface / lamellipodium assembly / regulation of focal adhesion assembly / maintenance of blood-brain barrier / stress fiber assembly / cell-substrate adhesion / brush border / Signaling by ALK fusions and activated point mutants / Smooth Muscle Contraction / positive regulation of glycogen biosynthetic process / positive regulation of lipid biosynthetic process / stress fiber / positive regulation of insulin receptor signaling pathway / cytoskeletal protein binding / cell-matrix adhesion / negative regulation of cell migration / cell projection / morphogenesis of an epithelium / positive regulation of protein localization to plasma membrane / adherens junction / positive regulation of glucose import / sarcolemma / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / insulin receptor binding / platelet aggregation / beta-catenin binding / nuclear matrix / cellular response to insulin stimulus / specific granule lumen / Signaling by RAF1 mutants / extracellular vesicle / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / cell-cell junction / Signaling by BRAF and RAF1 fusions / signaling receptor complex adaptor activity / Platelet degranulation / insulin receptor signaling pathway / actin binding / secretory granule lumen / ficolin-1-rich granule lumen / molecular adaptor activity / cytoskeleton / cell adhesion / cadherin binding / membrane raft / focal adhesion / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / structural molecule activity / protein-containing complex / extracellular exosome / extracellular region / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.41 Å | ||||||
Authors | Zhao, D. / Li, F. / Wu, J. / Shi, Y. / Zhang, Z. / Gong, Q. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2014 Title: Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin Authors: Zhao, D. / Wang, X. / Peng, J. / Wang, C. / Li, F. / Sun, Q. / Zhang, Y. / Zhang, J. / Cai, G. / Zuo, X. / Wu, J. / Shi, Y. / Zhang, Z. / Gong, Q. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4lnp.cif.gz | 45.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4lnp.ent.gz | 33 KB | Display | PDB format |
PDBx/mmJSON format | 4lnp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ln/4lnp ftp://data.pdbj.org/pub/pdb/validation_reports/ln/4lnp | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 7257.308 Da / Num. of mol.: 1 Fragment: protein-protein binding domain, UNP residues 794-854 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KIAA0894, KIAA1296, SH3D5, SORBS1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9BX66 |
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#2: Protein/peptide | Mass: 1083.257 Da / Num. of mol.: 1 / Fragment: proline rich peptide, UNP residues 870-879 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VCL / Production host: Escherichia coli (E. coli) / References: UniProt: P18206 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.95 % |
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Crystal grow | Temperature: 293 K / Method: evaporation / pH: 8 / Details: pH 8.0, EVAPORATION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 77 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.41→38.06 Å / Num. all: 14294 / Num. obs: 13539 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.41→38.06 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.955 / SU B: 2.613 / SU ML: 0.045 / Cross valid method: THROUGHOUT / ESU R: 0.063 / ESU R Free: 0.064 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.041 Å2
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Refinement step | Cycle: LAST / Resolution: 1.41→38.06 Å
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