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Open data
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Basic information
Entry | Database: PDB / ID: 6cgt | |||||||||
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Title | HOXA COMPLEX OF CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT | |||||||||
![]() | CYCLODEXTRIN GLYCOSYLTRANSFERASE | |||||||||
![]() | GLYCOSYLTRANSFERASE / STARCH DEGRADATION / CYCLODEXTRIN | |||||||||
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 | ![]() | |||||||||
![]() | Parsiegla, G. / Schulz, G.E. | |||||||||
![]() | ![]() Title: Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production. Authors: Parsiegla, G. / Schmidt, A.K. / Schulz, G.E. #1: ![]() Title: Structure of Cyclodextrin Glycosyltransferase Complexed with a Derivative of its Main Product Beta-Cyclodextrin Authors: Schmidt, A.K. / Cottaz, S. / Driguez, H. / Schulz, G.E. #2: ![]() Title: Catalytic Center of Cyclodextrin Glycosyltransferase Derived from X-Ray Structure Analysis Combined with Site-Directed Mutagenesis Authors: Klein, C. / Hollender, J. / Bender, H. / Schulz, G.E. #3: ![]() Title: Structure of Cyclodextrin Glycosyltransferase Refined at 2.0 A Resolution Authors: Klein, C. / Schulz, G.E. #4: ![]() Title: Molecular Cloning, Nucleotide Sequence and Expression in Escherichia Coli of the Beta-Cyclodextrin Glycosyltransferase Gene from Bacillus Circulans Strain No. 8 Authors: Nitschke, L. / Heeger, K. / Bender, H. / Schulz, G.E. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 143.7 KB | Display | ![]() |
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PDB format | ![]() | 116.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1010.5 KB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 28.3 KB | Display | |
Data in CIF | ![]() | 40.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 74552.984 Da / Num. of mol.: 1 / Mutation: L194T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P30920, cyclomaltodextrin glucanotransferase | ||||||
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#2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.73 Å3/Da / Density % sol: 67 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.9 / Details: pH 6.9 | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.7 / Method: vapor diffusion, hanging drop / Details: Hofmann, B.E., (1989) J.Mol.Biol., 209, 793. | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jul 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→27.4 Å / Num. obs: 30356 / % possible obs: 92 % / Rsym value: 0.087 |
Reflection shell | Highest resolution: 2.6 Å / % possible all: 69 |
Reflection | *PLUS Rmerge(I) obs: 0.087 |
Reflection shell | *PLUS % possible obs: 69 % |
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Processing
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Refinement | Method to determine structure: X-PLOR WITH WILD-TYPE MODEL / Resolution: 2.6→27 Å / Cross valid method: THROUGHOUT
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Displacement parameters | Biso mean: 16.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→27 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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