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- PDB-1ukq: Crystal structure of cyclodextrin glucanotransferase complexed wi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ukq | ||||||||||||
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Title | Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose | ||||||||||||
![]() | Cyclomaltodextrin glucanotransferase | ||||||||||||
![]() | TRANSFERASE / CGTASE / ACARBOSE / CARBOHYDRATE-PROTEIN COMPLEX | ||||||||||||
Function / homology | ![]() cyclomaltodextrin glucanotransferase / cyclomaltodextrin glucanotransferase activity / starch binding / alpha-amylase activity / carbohydrate metabolic process / extracellular region / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Haga, K. / Kanai, R. / Sakamoto, O. / Harata, K. / Yamane, K. | ||||||||||||
![]() | ![]() Title: Effects of Essential Carbohydrate/Aromatic Stacking Interaction with Tyr100 and Phe259 on Substrate Binding of Cyclodextrin Glycosyltransferase from Alkalophilic Bacillus sp. 1011 Authors: Haga, K. / Kanai, R. / Sakamoto, O. / Aoyagi, M. / Harata, K. / Yamane, K. #1: ![]() Title: X-ray Structure of Cyclodextrin Glucano-transferase from Alkalophilic Bacillus sp.1011. Comparison of Two Independent Molecules at 1.8 Angstrom Resolution Authors: Harata, K. / Haga, K. / Nakamura, A. / Aoyagi, M. / Yamane, K. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 290.4 KB | Display | ![]() |
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PDB format | ![]() | 230.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 56.5 KB | Display | |
Data in CIF | ![]() | 80.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1uksC ![]() 1uktC ![]() 1pamS 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
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 75230.086 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P05618, cyclomaltodextrin glucanotransferase |
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-Sugars , 3 types, 4 molecules ![](data/chem/img/GLC.gif)
#2: Polysaccharide | alpha-D-quinovopyranose-(1-4)-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#3: Polysaccharide | alpha-D-quinovopyranose-(1-4)-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Sugar |
-Non-polymers , 3 types, 644 molecules ![](data/chem/img/ACI.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | #6: Chemical | ChemComp-CA / #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 45.64 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: PEG 3000, sodium citrate, 2-propanol, calcium chloride, acarbose, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystal grow | *PLUS Method: unknown / Details: Harata, K., (1996) Acta Cryst., D52, 1136. |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: BRUKER SMART 6000 / Detector: CCD / Date: Oct 22, 2001 |
Radiation | Monochromator: OSMIC MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→48.554 Å / Num. all: 117580 / Num. obs: 91157 / % possible obs: 96 % / Observed criterion σ(F): 20.96 / Rmerge(I) obs: 0.132 |
Reflection shell | Resolution: 2→2.039 Å / Rmerge(I) obs: 0.245 / Num. unique all: 4609 / % possible all: 86.97 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 48.55 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1PAM Resolution: 2→10 Å / Isotropic thermal model: Isotropic / σ(F): 1 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 6
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Refine LS restraints | *PLUS
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