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- PDB-1ffw: CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY WITH A BOUND IMI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ffw | ||||||
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Title | CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY WITH A BOUND IMIDO DIPHOSPHATE | ||||||
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![]() | TRANSFERASE/SIGNALING PROTEIN / doubly wound (beta/alpha)5 fold / TRANSFERASE-SIGNALING PROTEIN COMPLEX | ||||||
Function / homology | ![]() negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / 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 / protein histidine kinase activity / bacterial-type flagellum ...negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / 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 / protein histidine kinase activity / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / histidine kinase / phosphorelay sensor kinase activity / acetyltransferase activity / phosphorelay signal transduction system / establishment of localization in cell / chemotaxis / magnesium ion binding / signal transduction / ATP binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gouet, P. / Chinardet, N. / Welch, M. / Guillet, V. / Birck, C. / Mourey, L. / Samama, J.-P. | ||||||
![]() | ![]() Title: Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex. Authors: Gouet, P. / Chinardet, N. / Welch, M. / Guillet, V. / Cabantous, S. / Birck, C. / Mourey, L. / Samama, J.-P. #1: ![]() Title: Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY Authors: WELCH, M. / CHINARDET, N. / MOUREY, L. / BIRCK, C. / SAMAMA, J.-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 | ![]() | 91.5 KB | Display | ![]() |
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PDB format | ![]() | 68.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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: 13981.136 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; CELLULAR_LOCATION: CYTOPLASM; EXPRESSION_SYSTEM: ESCHERICHIA COLI; Cellular location (production host): CYTOPLASM / Production host: ![]() ![]() #2: Protein | Mass: 14479.338 Da / Num. of mol.: 2 / Fragment: RESIDUES 124-257 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P07363, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a nitrogenous group as acceptor #3: Chemical | #4: Chemical | ChemComp-PON / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.67 % |
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Crystal grow | Temperature: 297 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER 0.02 M DTT, 0.01 M MANGANESE CHLORIDE, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
Crystal grow | *PLUS Details: Welch, M., (1998) Nature Struct. Biol., 5, 25. |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Oct 14, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. all: 35121 / Num. obs: 16044 / % possible obs: 85.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 2.2 % / Biso Wilson estimate: 52 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 2 % / Rmerge(I) obs: 0.191 / % possible all: 88.8 |
Reflection shell | *PLUS % possible obs: 88.8 % / Redundancy: 2.1 % |
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Processing
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Refinement | Resolution: 2.7→15 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.7→15 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 15 Å / σ(F): 0 / Rfactor obs: 0.213 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.3 |