+Open data
-Basic information
Entry | Database: PDB / ID: 1e6m | ||||||
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Title | TWO-COMPONENT SIGNAL TRANSDUCTION SYSTEM D57A MUTANT OF CHEY | ||||||
Components | CHEMOTAXIS PROTEIN CHEY | ||||||
Keywords | SIGNALING PROTEIN / TWO-COMPONENT SIGNAL TRANSDUCTION SYSTEM / CHEMOTAXIS / ACTIVE SITE MUTANT | ||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity ...bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / acetyltransferase activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI K-12 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Sola, M. / Lopez-Hernandez, E. / Cronet, P. / Lacroix, E. / Serrano, L. / Coll, M. / Parraga, A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY. Authors: Sola, M. / Lopez-Hernandez, E. / Cronet, P. / Lacroix, E. / Serrano, L. / Coll, M. / Parraga, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e6m.cif.gz | 33.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e6m.ent.gz | 25.2 KB | Display | PDB format |
PDBx/mmJSON format | 1e6m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e6/1e6m ftp://data.pdbj.org/pub/pdb/validation_reports/e6/1e6m | 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: 13953.126 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI K-12 (bacteria) / Plasmid: VECTOR DERIVED FROM PTZ 18 U / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): JM109 / References: UniProt: P0AE67 |
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#2: Water | ChemComp-HOH / |
Compound details | CHAIN A ENGINEERED MUTATION ASP57ALA TRANSMISSION OF SENSORY SIGNALS FROM THE CHEMORECEPTORS TO THE ...CHAIN A ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.92 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: pH 7.00 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 0.993 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.993 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. obs: 8189 / % possible obs: 90.8 % / Observed criterion σ(I): 2 / Redundancy: 3.1 % / Rmerge(I) obs: 0.051 / Rsym value: 0.079 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.3 Å / % possible obs: 84.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→10 Å / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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