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- PDB-2gbp: SUGAR AND SIGNAL-TRANSDUCER BINDING SITES OF THE ESCHERICHIA COLI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2gbp | ||||||
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Title | SUGAR AND SIGNAL-TRANSDUCER BINDING SITES OF THE ESCHERICHIA COLI GALACTOSE CHEMORECEPTOR PROTEIN | ||||||
![]() | D-GALACTOSE/D-GLUCOSE BINDING PROTEIN | ||||||
![]() | PERIPLASMIC BINDING PROTEIN | ||||||
Function / homology | ![]() methylgalactoside transport / galactose transmembrane transport / carbohydrate transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / chemotaxis / outer membrane-bounded periplasmic space / carbohydrate binding / periplasmic space / calcium ion binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Vyas, N.K. / Vyas, M.N. / Quiocho, F.A. | ||||||
![]() | ![]() Title: Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Authors: Vyas, N.K. / Vyas, M.N. / Quiocho, F.A. #1: ![]() Title: A Novel Calcium Binding Site in the Galactose-Binding Protein of Bacterial Transport and Chemotaxis Authors: Vyas, N.K. / Vyas, M.N. / Quiocho, F.A. #2: ![]() Title: The 3 Angstroms Resolution Structure of a D-Galactose-Binding Protein for Transport and Chemotaxis in Escherichia Coli Authors: Vyas, N.K. / Vyas, M.N. / Quiocho, F.A. #3: ![]() Title: Preliminary Crystallographic Data of Receptors for Transport and Chemotaxis in Escherichia Coli. D-Galactose and Maltose-Binding Proteins Authors: Quiocho, F.A. / Meador, W.E. / Pflugrath, J.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.8 KB | Display | ![]() |
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PDB format | ![]() | 56.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 387.7 KB | Display | ![]() |
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Full document | ![]() | 401.7 KB | Display | |
Data in XML | ![]() | 9.7 KB | Display | |
Data in CIF | ![]() | 14.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 33407.625 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Sugar | ChemComp-BGC / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.96 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.9 / Method: microdialysisDetails: referred to 'Quiocho, F.A.', (1979) J.Mol.Biol., 133, 181-184 | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→10 Å /
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Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 10 Å / Num. reflection all: 19531 / Rfactor all: 0.146 / σ(I): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |