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- PDB-1pbg: THE THREE-DIMENSIONAL STRUCTURE OF 6-PHOSPHO-BETA GALACTOSIDASE F... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pbg | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURE OF 6-PHOSPHO-BETA GALACTOSIDASE FROM LACTOCOCCUS LACTIS | ||||||
![]() | 6-PHOSPHO-BETA-D-GALACTOSIDASE | ||||||
![]() | HYDROLASE (GLYCOSYL HYDROLASE) | ||||||
Function / homology | ![]() 6-phospho-beta-galactosidase / 6-phospho-beta-galactosidase activity / lactose catabolic process via tagatose-6-phosphate / beta-glucosidase activity / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Wiesmann, C. / Schulz, G.E. | ||||||
![]() | ![]() Title: The three-dimensional structure of 6-phospho-beta-galactosidase from Lactococcus lactis. Authors: Wiesmann, C. / Beste, G. / Hengstenberg, W. / Schulz, G.E. #1: ![]() Title: Identification of the Active-Site Nucleophile in 6-Phospho-Beta Galactosidase from Staphylococcus Aureus by Labelling with Synthetic Inhibitors Authors: Staedtler, P. / Hoenig, S. / Frank, R. / Withers, S.G. / Hengstenberg, W. #2: ![]() Title: 6-Phospho-Beta-Galactosidases of Gram-Positive and 6-Phospho-Beta-Glucosidase B of Gram-Negative Bacteria: Comparison of Structure and Function by Kinetic and Immunological Methods and ...Title: 6-Phospho-Beta-Galactosidases of Gram-Positive and 6-Phospho-Beta-Glucosidase B of Gram-Negative Bacteria: Comparison of Structure and Function by Kinetic and Immunological Methods and Mutagenesis of the Lacg Gene of Staphylococcus Aureus Authors: Witt, E. / Frank, R. / Hengstenberg, 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 | ![]() | 200.1 KB | Display | ![]() |
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PDB format | ![]() | 161.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar 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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Atom site foot note | 1: CIS PROLINE - PRO A 48 / 2: CIS PROLINE - PRO A 176 / 3: TRP A 421 - SER A 422 IS A CIS PEPTIDE. / 4: CIS PROLINE - PRO B 48 / 5: CIS PROLINE - PRO B 176 / 6: TRP B 421 - SER B 422 IS A CIS PEPTIDE. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.999948, -0.00719, 0.00717), Vector: |
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Components
#1: Protein | Mass: 54139.113 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: PRECIPITANT POLYETHYLENE GLYCOL Source: (gene. exp.) ![]() Strain: SUBSP. LACTIS 712 / Description: DELTA H DELTA 1TRP / Gene: LACG / Plasmid: PNZ316 / Gene (production host): LACG / Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Compound details | SECONDARY STRUCTURE ASSIGNMENT WAS DONE BY THE PROGRAM DSSP. FOR A MANUAL ASSIGNMENT CHECK THE MOST ...SECONDARY STRUCTURE ASSIGNMENT | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.81 % | ||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 50 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 8 / PH range high: 6.7 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→100 Å / Num. obs: 36765 / % possible obs: 78.8 % / Redundancy: 3 % / Rmerge(I) obs: 0.069 |
Reflection | *PLUS Observed criterion σ(I): 0 / Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Resolution: 2.3→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 19.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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