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- PDB-4ha1: MutB inactive double mutant D200A-D415N in complex with isomaltulose -
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Open data
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Basic information
Entry | Database: PDB / ID: 4ha1 | |||||||||
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Title | MutB inactive double mutant D200A-D415N in complex with isomaltulose | |||||||||
![]() | Sucrose isomerase | |||||||||
![]() | ISOMERASE / ISOMALTULOSE SYNTHASE LIKE / TIM-BARREL / (BETA/ALPHA)8 / SUCROSE ISOMERASE / GLYCOSIDE HYDROLASE / TREHALULOSE SYNTHASE / GH13 FAMILY (CAZY DATABASE) / CALCIUM BINDING | |||||||||
Function / homology | ![]() glucan 1,4-alpha-maltotriohydrolase activity / oligo-1,6-glucosidase activity / maltose catabolic process / : / sucrose alpha-glucosidase activity / sucrose catabolic process / alpha-amylase activity / amino acid transport / isomerase activity / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Lipski, A. / Haser, R. / Aghajari, N. | |||||||||
![]() | ![]() Title: Insights into product binding in sucrose isomerases from crystal structures of MutB from Rhizobium sp. Authors: Lipski, A. / Watzlawick, H. / Ravaud, S. / Robert, X. / Haser, R. / Mattes, R. / Aghajari, N. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 263.1 KB | Display | ![]() |
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PDB format | ![]() | 204.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 817.8 KB | Display | ![]() |
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Full document | ![]() | 825.1 KB | Display | |
Data in XML | ![]() | 51.7 KB | Display | |
Data in CIF | ![]() | 78.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4h7vC ![]() 4h8hC ![]() 4h8uC ![]() 4h8vC ![]() 2pwhS 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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Components
#1: Protein | Mass: 63893.855 Da / Num. of mol.: 2 / Fragment: TREHALULOSE SYNTHASE MUTB, UNP residues 28-584 / Mutation: D200A, D415N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q2PS28, UniProt: M1E1F6*PLUS, EC: 5.4.11.99 #2: Chemical | #3: Sugar | ChemComp-ISL / | #4: Sugar | ChemComp-GLC / | #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: 53.22 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 20% PEG10000, 0.1M TRIS-HCL , pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 26, 2009 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→43.4 Å / Num. all: 66205 / Num. obs: 64580 / % possible obs: 97.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 3.1 % / Biso Wilson estimate: 24.39 Å2 / Rsym value: 0.165 / Net I/σ(I): 8.49 |
Reflection shell | Resolution: 2.2→2.5 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.441 / Mean I/σ(I) obs: 3.95 / % possible all: 97.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2PWH Resolution: 2.2→43.36 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.873 / SU ML: 0.28 / σ(F): 1.99 / Phase error: 27.4 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.44 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→43.36 Å
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Refine LS restraints |
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LS refinement shell |
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