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Yorodumi- PDB-2f9z: Complex between the chemotaxis deamidase CheD and the chemotaxis ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2f9z | ||||||
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Title | Complex between the chemotaxis deamidase CheD and the chemotaxis phosphatase CheC from Thermotoga maritima | ||||||
Components |
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Keywords | SIGNALING PROTEIN / bacterial chemotaxis / signal transduction / receptor deamidase / aspartyl phosphatase / protein complex / reciprocal regulation | ||||||
Function / homology | Function and homology information protein-glutamate methylesterase / protein-glutamate methylesterase activity / protein-glutamine glutaminase activity / protein-glutamine glutaminase / Hydrolases / chemotaxis / hydrolase activity Similarity search - Function | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Chao, X. / Park, S.Y. / Bilwes, A.M. / Crane, B.R. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2006 Title: A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation. Authors: Chao, X. / Muff, T.J. / Park, S.Y. / Zhang, S. / Pollard, A.M. / Ordal, G.W. / Bilwes, A.M. / Crane, B.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2f9z.cif.gz | 149.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2f9z.ent.gz | 116.9 KB | Display | PDB format |
PDBx/mmJSON format | 2f9z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2f9z_validation.pdf.gz | 426.3 KB | Display | wwPDB validaton report |
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Full document | 2f9z_full_validation.pdf.gz | 454 KB | Display | |
Data in XML | 2f9z_validation.xml.gz | 19 KB | Display | |
Data in CIF | 2f9z_validation.cif.gz | 29.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f9/2f9z ftp://data.pdbj.org/pub/pdb/validation_reports/f9/2f9z | HTTPS FTP |
-Related structure data
Related structure data | 1xkrS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 22567.336 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Strain: MSB8 / Gene: TM0904 / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9X006 #2: Protein | Mass: 16893.930 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Strain: MSB8 / Gene: TM0903 / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9X005 #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: 2.58 Å3/Da / Density % sol: 52.37 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 30% PEG 4000, 0.1M Tris, 0.25M Lithium Sulfate, 0.1M Cesium Chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F2 / Wavelength: 1.005 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 14, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.005 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→30 Å / Num. all: 32861 / Num. obs: 32861 / % possible obs: 93.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Biso Wilson estimate: 48.8 Å2 / Rsym value: 0.111 |
Reflection shell | Resolution: 2.4→2.48 Å / Rsym value: 0.306 / % possible all: 89.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1XKR Resolution: 2.4→30 Å / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.4→30 Å
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Refine LS restraints |
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