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Yorodumi- PDB-2z17: Crystal structure of PDZ domain from human Pleckstrin homology, Sec7 -
+Open data
-Basic information
Entry | Database: PDB / ID: 2z17 | ||||||
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Title | Crystal structure of PDZ domain from human Pleckstrin homology, Sec7 | ||||||
Components | Pleckstrin homology Sec7 and coiled-coil domains-binding protein | ||||||
Keywords | PROTEIN BINDING / PDZ domain / Coiled coil / Cytoplasm / Membrane / Polymorphism / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information regulation of cell adhesion / cell cortex / early endosome / nucleoplasm / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.7 Å | ||||||
Authors | Kishishita, S. / Nishino, A. / Murayama, K. / Terada, T. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Crystal structure of PDZ domain from human Pleckstrin homology, Sec7 Authors: Kishishita, S. / Nishino, A. / Murayama, K. / Terada, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2z17.cif.gz | 31 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2z17.ent.gz | 20.6 KB | Display | PDB format |
PDBx/mmJSON format | 2z17.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z1/2z17 ftp://data.pdbj.org/pub/pdb/validation_reports/z1/2z17 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 11304.448 Da / Num. of mol.: 1 / Fragment: PDZ domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PK060110-70 / Production host: Cell-free protein synthesis / References: UniProt: O60759 |
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#2: 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: 2.25 Å3/Da / Density % sol: 45.32 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.1M HEPES-Na, 2.0M Ammonium Sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 0.9789, 0.9794, 0.964 | ||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 11, 2006 / Details: mirrors | ||||||||||||
Radiation | Monochromator: Si II / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.5→50 Å / Num. obs: 3931 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 19.5 % / Biso Wilson estimate: 38.2 Å2 / Rsym value: 0.061 / Net I/σ(I): 41.9 | ||||||||||||
Reflection shell | Resolution: 2.5→2.63 Å / Mean I/σ(I) obs: 15.6 / Rsym value: 0.232 / % possible all: 99.6 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.7→28.54 Å / Rfactor Rfree error: 0.015 / Data cutoff high absF: 145252.75 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 46.1437 Å2 / ksol: 0.340996 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→28.54 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.87 Å / Rfactor Rfree error: 0.07 / Total num. of bins used: 6
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Xplor file |
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