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Yorodumi- PDB-1a47: CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1a47 | ||||||||||||
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Title | CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR | ||||||||||||
Components | CYCLODEXTRIN GLYCOSYLTRANSFERASE | ||||||||||||
Keywords | GLYCOSIDASE / THERMOSTABLE / FAMILY 13 GLYCOSYL HYDROLASE / LIGAND / SUBSTRATE / ACARBOSE | ||||||||||||
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 / MOLECULAR REPLACEMENT / Resolution: 2.56 Å | ||||||||||||
Authors | Uitdehaag, J.C.M. / Kalk, K.H. / Rozeboom, H.J. / Dijkstra, B.W. | ||||||||||||
Citation | Journal: J.Biol.Chem. / Year: 1998 Title: Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. Authors: Wind, R.D. / Uitdehaag, J.C. / Buitelaar, R.M. / Dijkstra, B.W. / Dijkhuizen, L. #1: Journal: J.Mol.Biol. / Year: 1996 Title: Crystal Structure at 2.3 A Resolution and Revised Nucleotide Sequence of the Thermostable Cyclodextrin Glycosyltransferase from Thermoanaerobacterium Thermosulfurigenes Em1 Authors: Knegtel, R.M. / Wind, R.D. / Rozeboom, H.J. / Kalk, K.H. / Buitelaar, R.M. / Dijkhuizen, L. / Dijkstra, B.W. #2: Journal: Biochemistry / Year: 1996 Title: Structure of Cyclodextrin Glycosyltransferase Complexed with a Maltononaose Inhibitor at 2.6 Angstrom Resolution. Implications for Product Specificity Authors: Strokopytov, B. / Knegtel, R.M. / Penninga, D. / Rozeboom, H.J. / Kalk, K.H. / 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 | 1a47.cif.gz | 149.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a47.ent.gz | 117.5 KB | Display | PDB format |
PDBx/mmJSON format | 1a47.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a4/1a47 ftp://data.pdbj.org/pub/pdb/validation_reports/a4/1a47 | HTTPS FTP |
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-Related structure data
Related structure data | 1ciuS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 75498.078 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermoanaerobacterium thermosulfurigenes (bacteria) Strain: EM1 / Cellular location: EXTRACELLULARGlossary of biology / Gene: AMYA / Plasmid: PCT2 / Cellular location (production host): EXTRACELLULAR / Gene (production host): AMYA / Production host: Escherichia coli (E. coli) / Strain (production host): PC1990 References: UniProt: P26827, cyclomaltodextrin glucanotransferase |
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-Sugars , 3 types, 3 molecules
#2: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltotriose |
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#3: Polysaccharide | alpha-D-quinovopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Polysaccharide | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose |
-Non-polymers , 3 types, 188 molecules
#5: Chemical | ChemComp-ADH / | ||
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#6: Chemical | #7: Water | ChemComp-HOH / | |
-Details
Compound details | ELECTRON DENSITY IN THE ACTIVE SITE, BETWEEN SUBSITES -1 AND +1 (THE SCISSILE BOND), IS NOT ...ELECTRON DENSITY IN THE ACTIVE SITE, BETWEEN SUBSITES -1 AND +1 (THE SCISSILE BOND), IS NOT COMPATIBLE |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.1 % | |||||||||||||||
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Crystal grow | pH: 7.7 Details: 21% SATURATED AMMONIUM SULFATE, 100 MM TRIS, PH 7.7 | |||||||||||||||
Crystal grow | *PLUS pH: 7.6 / Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-21 / Wavelength: 1.5418 |
Detector | Type: MAC Science DIP-2020 / Detector: IMAGE PLATE / Date: Apr 8, 1996 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.56→45.07 Å / Num. obs: 25423 / % possible obs: 91.1 % / Observed criterion σ(I): 2 / Redundancy: 5.9 % / Biso Wilson estimate: 17.9 Å2 / Rmerge(I) obs: 0.0682 / Rsym value: 0.07 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 2.56→2.58 Å / Redundancy: 3 % / Rmerge(I) obs: 0.2155 / Mean I/σ(I) obs: 4.9 / Rsym value: 0.22 / % possible all: 74.3 |
Reflection | *PLUS Num. measured all: 181769 |
Reflection shell | *PLUS % possible obs: 74.3 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1CIU Resolution: 2.56→8 Å / Isotropic thermal model: TNT BCORREL / Cross valid method: R FREE THROUGHOUT / σ(F): 0 / Stereochemistry target values: TNT PROTGEO Details: IDEAL PARAMETERS FOR GLUCOSE FROM TAKUSAGAWA & JACOBSON (1978), ACTA CRYST. B34:213-218, FOR ACARBOSE FROM STROKOPYTOV ET AL. (1995) BIOCHEMISTRY 34:2234-2240
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Refinement step | Cycle: LAST / Resolution: 2.56→8 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5D / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.186 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 17.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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