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Yorodumi- PDB-4cgt: DELETION MUTANT DELTA(145-150), F151D OF CYCLODEXTRIN GLYCOSYLTRA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4cgt | ||||||
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Title | DELETION MUTANT DELTA(145-150), F151D OF CYCLODEXTRIN GLYCOSYLTRANSFERASE | ||||||
Components | CYCLODEXTRIN GLYCOSYLTRANSFERASE | ||||||
Keywords | GLYCOSYLTRANSFERASE / STARCH DEGRADATION / CYCLODEXTRIN | ||||||
Function / homology | Function and homology information cyclomaltodextrin glucanotransferase / cyclomaltodextrin glucanotransferase activity / starch binding / alpha-amylase activity / carbohydrate metabolic process / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus circulans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / X-PLOR / Resolution: 2.6 Å | ||||||
Authors | Parsiegla, G. / Schulz, G.E. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 1998 Title: Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production. Authors: Parsiegla, G. / Schmidt, A.K. / Schulz, G.E. #1: Journal: Biochemistry / Year: 1998 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: Journal: Biochemistry / Year: 1992 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: Journal: J.Mol.Biol. / Year: 1991 Title: Structure of Cyclodextrin Glycosyltransferase Refined at 2.0 A Resolution Authors: Klein, C. / Schulz, G.E. #4: Journal: Appl.Microbiol.Biotechnol. / Year: 1990 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4cgt.cif.gz | 143.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4cgt.ent.gz | 110 KB | Display | PDB format |
PDBx/mmJSON format | 4cgt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4cgt_validation.pdf.gz | 414.9 KB | Display | wwPDB validaton report |
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Full document | 4cgt_full_validation.pdf.gz | 432.7 KB | Display | |
Data in XML | 4cgt_validation.xml.gz | 26.9 KB | Display | |
Data in CIF | 4cgt_validation.cif.gz | 38.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cg/4cgt ftp://data.pdbj.org/pub/pdb/validation_reports/cg/4cgt | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 73868.266 Da / Num. of mol.: 1 / Mutation: DEL(145-150), F151D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus circulans (bacteria) / Strain: 8 / Cellular location: EXTRACELLULAR / Production host: Escherichia coli (E. coli) / Strain (production host): TG1 References: UniProt: P30920, cyclomaltodextrin glucanotransferase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.79 Å3/Da / Density % sol: 68 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.9 / Details: pH 6.9 | |||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||
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: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Sep 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→26.63 Å / Num. obs: 30720 / % possible obs: 88 % / Rsym value: 0.111 |
-Processing
Software |
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Refinement | Method to determine structure: X-PLOR Starting model: WILD-TYPE WITH RESIDUES 145 - 151 DELETED Resolution: 2.6→10 Å / Cross valid method: THROUGHOUT
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Displacement parameters | Biso mean: 12.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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