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Open data
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Basic information
Entry | Database: PDB / ID: 3t2o | ||||||
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Title | E. coli (lacZ) beta-galactosidase (S796D) | ||||||
![]() | Beta-galactosidase | ||||||
![]() | HYDROLASE / Dynamic Loop Conformation / Ser-796 / TIM BARREL (ALPHA/BETA BARREL) / JELLY-ROLL BARREL / IMMUNOGLOBULIN / BETA SUPERSANDWICH / GLYCOSIDASE | ||||||
Function / homology | ![]() alkali metal ion binding / lactose catabolic process / beta-galactosidase complex / beta-galactosidase / beta-galactosidase activity / carbohydrate binding / magnesium ion binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Jancewicz, L.J. / Wheatley, R.W. / Sutendra, G. / Lee, M. / Fraser, M. / Huber, R.E. | ||||||
![]() | ![]() Title: Ser-796 of Beta-Galactosidase (E. coli) Plays a Key Role in Maintaining an Optimum Balance between the Opened and Closed Conformations of the Catalytically Important Active Site Loop Authors: Jancewicz, L.J. / Wheatley, R.W. / Sutendra, G. / Lee, M. / Fraser, M.E. / Huber, R.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 949.3 KB | Display | ![]() |
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PDB format | ![]() | 754.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 511.5 KB | Display | ![]() |
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Full document | ![]() | 534.7 KB | Display | |
Data in XML | ![]() | 178.1 KB | Display | |
Data in CIF | ![]() | 274.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3sepC ![]() 3t08C ![]() 3t09C ![]() 3t0aC ![]() 3t0bC ![]() 3t0dC ![]() 3t2pC ![]() 3t2qC C: citing same article ( |
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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: 119771.758 Da / Num. of mol.: 4 / Fragment: Unp residues 10-1024 / Mutation: S796D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-NA / #4: Chemical | ChemComp-DMS / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.25 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 8-10% PEG 8000, 100 MM BIS-TRIS, 200 MM MGCL2, 100 MM NACL, 10 MM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 288.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 1, 2007 / Details: KOHZU Double Crystal Si(111) |
Radiation | Monochromator: Double flat crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.11587 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→200 Å / Num. all: 425379 / Num. obs: 425379 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Biso Wilson estimate: 18 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 19 |
Reflection shell | Resolution: 1.85→1.88 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.475 / Mean I/σ(I) obs: 2.2 / Num. unique all: 20163 / % possible all: 95.2 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.685 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→61.03 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.85→1.898 Å / Total num. of bins used: 20
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