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Yorodumi- PDB-1ciu: THERMOSTABLE CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ciu | ||||||
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Title | THERMOSTABLE CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 AT PH 8.0. | ||||||
Components | CYCLODEXTRIN GLYCOSYLTRANSFERASE | ||||||
Keywords | GLYCOSIDASE / THERMOSTABLE | ||||||
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 | Thermoanaerobacterium thermosulfurigenes (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Knegtel, R.M.A. / Dijkstra, B.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1. Authors: Knegtel, R.M. / Wind, R.D. / Rozeboom, H.J. / Kalk, K.H. / Buitelaar, R.M. / Dijkhuizen, L. / Dijkstra, B.W. #1: Journal: Biochemistry / Year: 1995 Title: X-Ray Structure of Cyclodextrin Glycosyltransferase Complexed with Acarbose. Implications for the Catalytic Mechanism of Glycosidases Authors: Strokopytov, B. / Penninga, D. / Rozeboom, H.J. / Kalk, K.H. / Dijkhuizen, L. / Dijkstra, B.W. #2: Journal: J.Mol.Biol. / Year: 1994 Title: Nucleotide Sequence and X-Ray Structure of Cyclodextrin Glycosyltransferase from Bacillus Circulans Strain 251 in a Maltose-Dependent Crystal Form Authors: Lawson, C.L.L. / Van Montfort, R. / Strokopytov, B. / Rozeboom, H.J. / Kalk, K.H. / De Vries, G.E. / Penninga, D. / Dijkhuizen, L. / Dijkstra, B.W. #3: Journal: J.Mol.Biol. / Year: 1990 Title: Maltodextrin-Dependent Crystallization of Cyclomalto-Dextrin Glucanotransferase from Bacillus Circulans Authors: Lawson, C.L.L. / Bergsma, J. / Bruinenberg, P.M. / De Vries, G. / Dijkhuizen, L. / Dijkstra, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ciu.cif.gz | 150.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ciu.ent.gz | 116.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ciu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ci/1ciu ftp://data.pdbj.org/pub/pdb/validation_reports/ci/1ciu | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-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 506 / 3: CIS PROLINE - PRO 621 / 4: CIS PROLINE - PRO 631 |
-Components
#1: Protein | Mass: 75498.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Thermoanaerobacterium thermosulfurigenes (bacteria) References: UniProt: P26827, cyclomaltodextrin glucanotransferase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.42 % | ||||||||||||||||||||
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Crystal | *PLUS Density % sol: 59 % | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 8 / PH range high: 7.6 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Jan 23, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Redundancy: 3.8 % / Rmerge(I) obs: 0.061 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 34.3 Å / Num. obs: 31189 / % possible obs: 82.4 % / Num. measured all: 119291 / Rmerge(I) obs: 0.061 |
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.34 Å / % possible obs: 66.6 % |
-Processing
Software |
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Refinement | Resolution: 2.3→6 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.249 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_plane_restr / Dev ideal: 0.009 |