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- PDB-1cgu: CATALYTIC CENTER OF CYCLODEXTRIN GLYCOSYLTRANSFERASE DERIVED FROM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cgu | |||||||||
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Title | CATALYTIC CENTER OF CYCLODEXTRIN GLYCOSYLTRANSFERASE DERIVED FROM X-RAY STRUCTURE ANALYSIS COMBINED WITH SITE-DIRECTED MUTAGENESIS | |||||||||
![]() | CYCLODEXTRIN GLYCOSYL-TRANSFERASE | |||||||||
![]() | GLYCOSYLTRANSFERASE | |||||||||
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 | ![]() | |||||||||
![]() | Klein, C. / Hollender, J. / Bender, H. / Schulz, G.E. | |||||||||
![]() | ![]() 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. #1: ![]() Title: Structure of Cyclodextrin Glycosyltransferase Refined at 2.0 Angstroms Resolution Authors: Klein, C. / Schulz, G.E. #2: ![]() Title: Engineering a Heavy Atom Derivative for the X-Ray Structure Analysis of Cyclodextrin Glycosyltransferase Authors: Klein, C. / Vogel, W. / Bender, H. / Schulz, G.E. #3: ![]() 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. #4: ![]() Title: Three-Dimensional Structure of Cyclodextrin Glycosyltransferase from Bacillus Circulans at 3.4 Angstroms Resolution Authors: Hofmann, B.E. / Bender, H. / Schulz, G.E. | |||||||||
History |
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Remark 650 | HELIX HELIX STRAND H1 IS A NONHELICAL SEGMENT BETWEEN ASP 63 AND ASN 64. | |||||||||
Remark 700 | SHEET THIS MOLECULE CONTAINS ONE BIFURCATED SHEET. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET ...SHEET THIS MOLECULE CONTAINS ONE BIFURCATED SHEET. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, THE TWO SHEETS, S11 AND S12, ARE DEFINED HAVING STRANDS 1, 2, 3, IN COMMON. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 151.4 KB | Display | ![]() |
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PDB format | ![]() | 119 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 787.9 KB | Display | ![]() |
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Full document | ![]() | 812.9 KB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 29.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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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Atom site foot note | 1: CIS PROLINE - PRO 372 / 2: CIS PROLINE - PRO 505 / 3: CIS PROLINE - PRO 623 / 4: CIS PROLINE - PRO 633 |
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Components
#1: Protein | Mass: 74521.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P30920, cyclomaltodextrin glucanotransferase | ||||
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#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE BELOW IS THAT DETERMINED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.77 Å3/Da / Density % sol: 67.41 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.7 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / % possible obs: 76 % / Rmerge(I) obs: 0.121 |
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Processing
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Refinement | Resolution: 2.5→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 10 Å / Num. reflection all: 28185 / σ(I): 0 / Rfactor all: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.6 |