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- PDB-1glg: CRYSTALLOGRAPHIC ANALYSIS OF THE EPIMERIC AND ANOMERIC SPECIFICIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1glg | ||||||
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Title | CRYSTALLOGRAPHIC ANALYSIS OF THE EPIMERIC AND ANOMERIC SPECIFICITY OF THE PERIPLASMIC TRANSPORT(SLASH)CHEMOTACTIC PROTEIN RECEPTOR FOR D-GLUCOSE AND D-GALACTOSE | ||||||
![]() | GALACTOSE/GLUCOSE-BINDING PROTEIN | ||||||
![]() | GALACTOSE-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, M.N. / Vyas, N.K. / Quiocho, F.A. | ||||||
![]() | ![]() Title: Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose. Authors: Vyas, M.N. / Vyas, N.K. / Quiocho, F.A. #1: ![]() Title: Comparison of the Periplasmic Receptors for L-Arabinose, D-Galactose, and D-Ribose Authors: Vyas, N.K. / Vyas, M.N. / Quiocho, F.A. #2: ![]() Title: Sugar and Signal-Transducer Binding Sites of the Escherichia Coli Galactose Receptor Protein Authors: Vyas, N.K. / Vyas, M.N. / Quiocho, F.A. #3: ![]() 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. | ||||||
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 KB | Display | ![]() |
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PDB format | ![]() | 56.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383 KB | Display | ![]() |
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Full document | ![]() | 389.3 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 12.6 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-GAL / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.59 % |
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Crystal grow | *PLUS Method: other / Details: Quiocho, F.A., (1979) J. Mol. Biol., 133, 181. |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. measured all: 19700 / Rmerge(I) obs: 0.059 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.07 Å |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→10 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 17.94 Å2 |