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- PDB-8ibt: Crystal structure of GH42 beta-galactosidase BiBga42A from Bifido... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8ibt | |||||||||||||||||||||
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Title | Crystal structure of GH42 beta-galactosidase BiBga42A from Bifidobacterium longum subspecies infantis E318S mutant in complex with lacto-N-tetraose | |||||||||||||||||||||
![]() | Beta-galactosidase | |||||||||||||||||||||
![]() | HYDROLASE / Glycoside Hydrolase family 42 | |||||||||||||||||||||
Function / homology | ![]() beta-galactosidase complex / beta-galactosidase / beta-galactosidase activity / carbohydrate metabolic process Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||||||||
![]() | Hidaka, M. / Fushinobu, S. / Gotoh, A. / Katayama, T. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Substrate recognition mode of a glycoside hydrolase family 42 beta-galactosidase from Bifidobacterium longum subspecies infantis ( Bi Bga42A) revealed by crystallographic and mutational analyses. Authors: Gotoh, A. / Hidaka, M. / Sakurama, H. / Nishimoto, M. / Kitaoka, M. / Sakanaka, M. / Fushinobu, S. / Katayama, T. #1: Journal: Glycobiology / Year: 2012 Title: Bifidobacterium longum subsp. infantis uses two different beta-galactosidases for selectively degrading type-1 and type-2 human milk oligosaccharides. Authors: Yoshida, E. / Sakurama, H. / Kiyohara, M. / Nakajima, M. / Kitaoka, M. / Ashida, H. / Hirose, J. / Katayama, T. / Yamamoto, K. / Kumagai, H. | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 296.8 KB | Display | ![]() |
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PDB format | ![]() | 236.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 8ibrC ![]() 8ibsC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 78764.820 Da / Num. of mol.: 2 / Mutation: E318S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 Gene: Blon_2016 / Production host: ![]() ![]() #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.8 Å3/Da / Density % sol: 67.67 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 5.8 Details: 5 mM MES-NaOH buffer (pH 5.8), 0.1 M KSCN, 30% PEG MME 2000, 20% ethylene glycol, 50 mM lacto-N-tetraose |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 27, 2014 |
Radiation | Monochromator: Numerical link type Si(111) double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→48.04 Å / Num. obs: 121062 / % possible obs: 100 % / Redundancy: 7.5 % / Biso Wilson estimate: 24.96 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.125 / Rpim(I) all: 0.074 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 2.2→2.24 Å / Rmerge(I) obs: 0.916 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 5977 / CC1/2: 0.633 / Rpim(I) all: 0.362 / % possible all: 99.9 |
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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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.356 Å2
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Refinement step | Cycle: 1 / Resolution: 2.2→48.04 Å
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Refine LS restraints |
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