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- PDB-4gi8: Crystal structure of the MUTB F164L mutant from crystals soaked w... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4gi8 | ||||||
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Title | Crystal structure of the MUTB F164L mutant from crystals soaked with the substrate sucrose | ||||||
![]() | Sucrose isomerase | ||||||
![]() | ISOMERASE / MUTANT ENZYME / 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 / maltose alpha-glucosidase activity / 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: Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity Authors: Lipski, A. / Watzlawick, H. / Ravaud, S. / Robert, X. / Rhimi, M. / 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 | ![]() | 261 KB | Display | ![]() |
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PDB format | ![]() | 207.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 454.7 KB | Display | ![]() |
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Full document | ![]() | 462.2 KB | Display | |
Data in XML | ![]() | 50.9 KB | Display | |
Data in CIF | ![]() | 77 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4gi6C ![]() 4gi9C ![]() 4giaC ![]() 4ginC ![]() 4h2cC ![]() 1zjbS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 63904.832 Da / Num. of mol.: 2 / Fragment: MUTB fragment, UNP residues 28-584 / Mutation: F164L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q2PS28, UniProt: M1E1F3*PLUS, EC: 5.4.11.99 #2: Chemical | #3: Chemical | ChemComp-GOL / #4: Chemical | ChemComp-TRS / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.34 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.1M Tris-HCl, 12%(w/v) PEG20000, 0.01M L-Cysteine, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 11, 2008 |
Radiation | Monochromator: YALE MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97559 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→48.92 Å / Num. all: 92762 / Num. obs: 91853 / % possible obs: 99 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 7.41 % / Biso Wilson estimate: 24.03 Å2 / Rsym value: 0.124 / Net I/σ(I): 11.74 |
Reflection shell | Resolution: 1.95→2.1 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.521 / Mean I/σ(I) obs: 4.02 / Num. unique all: 17461 / % possible all: 95.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ZJB Resolution: 1.95→48.92 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.958 / SU B: 2.962 / SU ML: 0.085 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R: 0.147 / ESU R Free: 0.132 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 17.73 Å2
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Refinement step | Cycle: LAST / Resolution: 1.95→48.92 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→2.003 Å / Total num. of bins used: 20
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