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- PDB-2vch: Characterization and engineering of the bifunctional N- and O- gl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vch | ||||||
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Title | Characterization and engineering of the bifunctional N- and O- glucosyltransferase involved in xenobiotic metabolism in plants | ||||||
![]() | HYDROQUINONE GLUCOSYLTRANSFERASE | ||||||
![]() | TRANSFERASE / GLYCOSYLTRANSFERASE / N-GLUCOSYLTRANSFERASE / UDP-GLUCOSE-DEPENDENT / PLANT GLYCOSYLTRANSFERASE / N-GLYCOSYLATION / O-GLYCOSYLATION / S-GLUCOSYLTRANSFERASE / O- GLUCOSYLTRANSFERASE | ||||||
Function / homology | ![]() hydroquinone glucosyltransferase / hydroquinone glucosyltransferase activity / lignin biosynthetic process / UDP-glucosyltransferase activity / UDP-glycosyltransferase activity / Transferases; Glycosyltransferases; Hexosyltransferases / xenobiotic catabolic process / xenobiotic metabolic process / response to toxic substance Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Brazier-Hicks, M. / Offen, W.A. / Gershater, M.C. / Revett, T.J. / Lim, E.K. / Bowles, D.J. / Davies, G.J. / Edwards, R. | ||||||
![]() | ![]() Title: Characterization and Engineering of the Bifunctional N- and O-Glucosyltransferase Involved in Xenobiotic Metabolism in Plants. Authors: Brazier-Hicks, M. / Offen, W.A. / Gershater, M.C. / Revett, T.J. / Lim, E.K. / Bowles, D.J. / Davies, G.J. / Edwards, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 116.7 KB | Display | ![]() |
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PDB format | ![]() | 87.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 796.2 KB | Display | ![]() |
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Full document | ![]() | 801.1 KB | Display | |
Data in XML | ![]() | 23.3 KB | Display | |
Data in CIF | ![]() | 36 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2vceC ![]() 2vg8C ![]() 1acvS 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
#1: Protein | Mass: 52992.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9M156, hydroquinone glucosyltransferase | ||
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#2: Chemical | ChemComp-UDP / | ||
#3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49 % / Description: NONE |
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Crystal grow | Details: 23 % (W/V) PEG 3350, 0.1 M MMT (MALIC ACID, MES, TRIS BUFFER) PH 8.0 |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 8, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.45→53.45 Å / Num. obs: 83274 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 4.2 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 1.45→1.53 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 5.5 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ACV Resolution: 1.45→53.45 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.952 / SU B: 0.951 / SU ML: 0.039 / Cross valid method: THROUGHOUT / ESU R: 0.068 / ESU R Free: 0.067 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-5, 50, 251-255, 318-319, 477-480 ARE DISORDERED
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.12 Å2
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Refinement step | Cycle: LAST / Resolution: 1.45→53.45 Å
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Refine LS restraints |
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