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Yorodumi- PDB-3sft: Crystal structure of Thermotoga maritima CheB methylesterase cata... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3sft | ||||||
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Title | Crystal structure of Thermotoga maritima CheB methylesterase catalytic domain | ||||||
Components | Chemotaxis response regulator protein-glutamate methylesterase | ||||||
Keywords | HYDROLASE / modified doubly-wound/fold / Methylesterase / chemoreceptor | ||||||
Function / homology | Function and homology information protein-glutamate methylesterase / protein-glutamate methylesterase activity / protein-glutamine glutaminase activity / protein-glutamine glutaminase / phosphorelay response regulator activity / chemotaxis / cytoplasm Similarity search - Function | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Park, S.Y. / Crane, B.R. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2011 Title: An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain Authors: Cho, K.H. / Crane, B.R. / Park, S.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3sft.cif.gz | 50.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3sft.ent.gz | 35.7 KB | Display | PDB format |
PDBx/mmJSON format | 3sft.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3sft_validation.pdf.gz | 419.3 KB | Display | wwPDB validaton report |
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Full document | 3sft_full_validation.pdf.gz | 419.7 KB | Display | |
Data in XML | 3sft_validation.xml.gz | 9.9 KB | Display | |
Data in CIF | 3sft_validation.cif.gz | 13.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sf/3sft ftp://data.pdbj.org/pub/pdb/validation_reports/sf/3sft | HTTPS FTP |
-Related structure data
Related structure data | 1chdS 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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Unit cell |
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-Components
#1: Protein | Mass: 20895.289 Da / Num. of mol.: 1 / Fragment: CheB methylesterase catalytic domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Gene: cheB / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: Q9WYN9, protein-glutamate methylesterase |
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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: 3.27 Å3/Da / Density % sol: 62.33 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.2M ammonium sulfate, 0.1M cacodylate, 30%(w/v) PEG 8K, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 23, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.15→30 Å / Num. obs: 13555 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1CHD Resolution: 2.15→30 Å
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Refinement step | Cycle: LAST / Resolution: 2.15→30 Å
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