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Open data
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Basic information
Entry | Database: PDB / ID: 5chy | ||||||
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Title | STRUCTURE OF CHEMOTAXIS PROTEIN CHEY | ||||||
![]() | CHEY | ||||||
![]() | SIGNAL TRANSDUCTION PROTEIN / RESPONSE REGULATORS / TWO-COMPONENT SYSTEMS | ||||||
Function / homology | ![]() 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 / histidine phosphotransfer kinase activity / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation ...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 / histidine phosphotransfer kinase activity / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / protein acetylation / phosphorelay signal transduction system / phosphorelay sensor kinase activity / acetyltransferase activity / chemotaxis / magnesium ion binding / signal transduction / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Zhu, X. / Rebello, J. / Matsumura, P. / Volz, K. | ||||||
![]() | ![]() Title: Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106. Authors: Zhu, X. / Rebello, J. / Matsumura, P. / Volz, K. #1: ![]() Title: Tyrosine 106 Plays an Important Role in Chemotaxis Signal Transduction in Escherichia Coli Authors: Zhu, X. / Amsler, C.D. / Volz, K. / Matsumura, P. #2: ![]() Title: Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis. The 2.1-A Structure of a Threonine to Isoleucine Mutant at Position 87 of Chey Authors: Ganguli, S. / Wang, H. / Matsumura, P. / Volz, K. #3: ![]() Title: Structural Conservation in the Chey Superfamily Authors: Volz, K. #4: ![]() Title: Crystal Structure of Escherichia Coli Chey Refined at 1.7-A Resolution Authors: Volz, K. / Matsumura, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 38.3 KB | Display | ![]() |
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PDB format | ![]() | 26.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433 KB | Display | ![]() |
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Full document | ![]() | 438.7 KB | Display | |
Data in XML | ![]() | 8.9 KB | Display | |
Data in CIF | ![]() | 11.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 14004.171 Da / Num. of mol.: 1 / Mutation: Y106W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.12 % | ||||||||||||||||||||
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Crystal grow | pH: 6 Details: 28% PEG 8000, 0.12 M CALCIUM ACETATE, 0.1 M CACODYLATE BUFFER, PH 6.0 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 292 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2 Å / Num. obs: 7433 / % possible obs: 92 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.066 / Net I/σ(I): 1 |
Reflection shell | Resolution: 2→2.13 Å / % possible all: 80.3 |
Reflection | *PLUS Num. measured all: 21022 |
Reflection shell | *PLUS % possible obs: 80.3 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 24.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.185 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.13 Å / Total num. of bins used: 7 / Num. reflection obs: 1357 / Rfactor obs: 0.278 |