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- PDB-1umz: Xyloglucan endotransglycosylase in complex with the xyloglucan no... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1umz | |||||||||
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Title | Xyloglucan endotransglycosylase in complex with the xyloglucan nonasaccharide XLLG. | |||||||||
![]() | XYLOGLUCAN ENDOTRANSGLYCOSYLASE | |||||||||
![]() | TRANSFERASE / GLYCOSIDE HYDROLASE / XET / XTH / XEH / TRANSGLYCOSYLATION / XYLOGLUCAN / GLYCOSYLTRANSFERASE | |||||||||
Function / homology | ![]() xyloglucan:xyloglucosyl transferase / xyloglucan:xyloglucosyl transferase activity / xyloglucan metabolic process / cell wall biogenesis / apoplast / polysaccharide binding / hydrolase activity, hydrolyzing O-glycosyl compounds / cell wall organization / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Johansson, P. / Brumer, H. / Kallas, A.M. / Henriksson, H. / Denman, S.E. / Teeri, T.T. / Jones, T.A. | |||||||||
![]() | ![]() Title: Crystal Structures of a Poplar Xyloglucan Endotransglycosylase Reveal Details of Transglycosylation Acceptor Binding Authors: Johansson, P. / Brumer, H. / Baumann, M.J. / Kallas, A.M. / Henriksson, H. / Denman, S.E. / Teeri, T.T. / Jones, T.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 134.4 KB | Display | ![]() |
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PDB format | ![]() | 105.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.9 MB | Display | ![]() |
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Full document | ![]() | 1.9 MB | Display | |
Data in XML | ![]() | 24.7 KB | Display | |
Data in CIF | ![]() | 35.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1un1SC S: Starting model for refinement 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.8446, 0.5335, 0.0456), Vector: |
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Components
#1: Protein | Mass: 32531.570 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q8GZD5, xyloglucan:xyloglucosyl transferase #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4 Å3/Da / Density % sol: 68 % | ||||||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 10 MG ML-1 PROTEIN SOLUTION 1:1 WITH 1.0 M NAOAC AND 0.2 M IMIDAZOLE PH 6.5 | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 15, 2002 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: DIAMOND (111), GE (220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. obs: 83886 / % possible obs: 96.7 % / Observed criterion σ(I): 2 / Redundancy: 3.61 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.8→1.83 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.662 / Mean I/σ(I) obs: 2 / % possible all: 71.7 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 29 Å / Redundancy: 3.61 % / Rmerge(I) obs: 0.063 |
Reflection shell | *PLUS % possible obs: 71.7 % / Rmerge(I) obs: 0.662 / Mean I/σ(I) obs: 2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1UN1 Resolution: 1.8→28.99 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.946 / Cross valid method: THROUGHOUT / ESU R: 0.106 / ESU R Free: 0.101 / 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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.91 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→28.99 Å
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Refine LS restraints |
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