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Yorodumi- PDB-1hey: INVESTIGATING THE STRUCTURAL DETERMINANTS OF THE P21-LIKE TRIPHOS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hey | ||||||
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Title | INVESTIGATING THE STRUCTURAL DETERMINANTS OF THE P21-LIKE TRIPHOSPHATE AND MG2+ BINDING SITE | ||||||
Components | CHEY | ||||||
Keywords | CHEMOTAXIS | ||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / aerotaxis / regulation of bacterial-type flagellum-dependent cell motility / 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 / aerotaxis / regulation of bacterial-type flagellum-dependent cell motility / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / protein acetylation / acetyltransferase activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.24 Å | ||||||
Authors | Bellsolell, L. / Coll, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Investigating the structural determinants of the p21-like triphosphate and Mg2+ binding site. Authors: Cronet, P. / Bellsolell, L. / Sander, C. / Coll, M. / Serrano, L. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Magnesium Binding to the Bacterial Chemotaxis Protein Chey Results in Large Conformational Changes Involving its Functional Surface Authors: Bellsolell, L. / Prieto, J. / Serrano, L. / Coll, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hey.cif.gz | 36.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hey.ent.gz | 25.3 KB | Display | PDB format |
PDBx/mmJSON format | 1hey.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hey_validation.pdf.gz | 405.8 KB | Display | wwPDB validaton report |
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Full document | 1hey_full_validation.pdf.gz | 407 KB | Display | |
Data in XML | 1hey_validation.xml.gz | 7.8 KB | Display | |
Data in CIF | 1hey_validation.cif.gz | 10 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/he/1hey ftp://data.pdbj.org/pub/pdb/validation_reports/he/1hey | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 110 |
-Components
#1: Protein | Mass: 13603.612 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.11 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X31 / Wavelength: 0.92 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 11, 1993 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Num. obs: 6707 / % possible obs: 90.7 % / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.111 |
Reflection | *PLUS Highest resolution: 2.24 Å / Num. measured all: 74759 / Rmerge(I) obs: 0.111 |
Reflection shell | *PLUS Highest resolution: 2.24 Å / Lowest resolution: 2.36 Å / % possible obs: 84.5 % |
-Processing
Software |
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Refinement | Resolution: 2.24→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 18 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.24→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.224 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |