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- PDB-4udj: Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylas... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4udj | ||||||
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Title | Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with beta-D-mannopyranose and inorganic phosphate | ||||||
![]() | UHGB_MP | ||||||
![]() | TRANSFERASE / GLYCOSIDE HYDROLASE FAMILY 130 / B-1 / 4-MANNOPYRANOSYL-CHITOBIOSE PHOSPHORYLASE / N-GLYCAN PHOSPHOROLYSIS | ||||||
Function / homology | ![]() | ||||||
Biological species | UNCULTURED ORGANISM (environmental samples) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ladeveze, S. / Cioci, G. / Potocki-Veronese, G. / Tranier, S. / Mourey, L. | ||||||
![]() | ![]() Title: Structural Bases for N-Glycan Processing by Mannoside Phosphorylase. Authors: Ladeveze, S. / Cioci, G. / Roblin, P. / Mourey, L. / Tranier, S. / Potocki-Veronese, G. #1: Journal: J.Biol.Chem. / Year: 2013 Title: Role of Glycoside Phosphorylases in Mannose Foraging by Human Gut Bacteria. Authors: Ladeveze, S. / Tarquis, L. / Cecchini, D.A. / Bercovici, J. / Andre, I. / Topham, C.M. / Morel, S. / Laville, E. / Monsan, P. / Lombard, V. / Henrissat, B. / Potocki-Veronese, G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 810.7 KB | Display | ![]() |
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PDB format | ![]() | 676.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 544.1 KB | Display | ![]() |
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Full document | ![]() | 566.2 KB | Display | |
Data in XML | ![]() | 83.4 KB | Display | |
Data in CIF | ![]() | 118.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4udgC ![]() 4udiSC ![]() 4udkC C: citing same article ( S: Starting model for refinement |
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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
-Protein / Sugars , 2 types, 12 molecules ABCDEF![](data/chem/img/BMA.gif)
![](data/chem/img/BMA.gif)
#1: Protein | Mass: 39321.422 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) UNCULTURED ORGANISM (environmental samples) Description: FECAL SAMPLE FROM HOMO SAPIENS / Plasmid: PET28A / Production host: ![]() ![]() References: UniProt: D9ZDQ9, Transferases; Glycosyltransferases; Hexosyltransferases #3: Sugar | ChemComp-BMA / |
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-Non-polymers , 5 types, 1207 molecules ![](data/chem/img/PO4.gif)
![](data/chem/img/K.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/K.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-PO4 / #4: Chemical | ChemComp-K / #5: Chemical | ChemComp-EDO / #6: Chemical | ChemComp-PGE / #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.82 % / Description: NONE |
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Crystal grow | pH: 7 Details: PROTEIN WAS CRYSTALLIZED FROM 17.5% PEG 3350, 200 MM NH4CL, pH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 26, 2014 / Details: PAIR OF KB MIRRORS FOR ADJUSTABLE FOCUSING |
Radiation | Monochromator: CHANNEL-CUT DOUBLE CRYSTAL MONOCHROMATOR (CINEL), CRYOCOOLED, 6MM GAP Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 |
Reflection | Resolution: 1.94→75 Å / Num. obs: 148390 / % possible obs: 99.7 % / Observed criterion σ(I): -1 / Redundancy: 8.2 % / Rmerge(I) obs: 0.16 / Net I/σ(I): 4 |
Reflection shell | Resolution: 1.94→2.04 Å / Redundancy: 7.9 % / Rmerge(I) obs: 0.59 / Mean I/σ(I) obs: 1.2 / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4UDI Resolution: 1.94→108.13 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.94 / SU B: 7.382 / SU ML: 0.094 / Cross valid method: THROUGHOUT / ESU R: 0.146 / ESU R Free: 0.134 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: 19.572 Å2
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Refinement step | Cycle: LAST / Resolution: 1.94→108.13 Å
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