+Open data
-Basic information
Entry | Database: PDB / ID: 1pam | ||||||
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Title | CYCLODEXTRIN GLUCANOTRANSFERASE | ||||||
Components | CYCLODEXTRIN GLUCANOTRANSFERASE | ||||||
Keywords | GLYCOSYLTRANSFERASE / TRANSFERASE | ||||||
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 sp. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Harata, K. / Haga, K. / Nakamura, A. / Aoyagi, M. / Yamane, K. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1996 Title: X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 A resolution. Authors: Harata, K. / Haga, K. / Nakamura, A. / Aoyagi, M. / Yamane, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pam.cif.gz | 288.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pam.ent.gz | 230 KB | Display | PDB format |
PDBx/mmJSON format | 1pam.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pa/1pam ftp://data.pdbj.org/pub/pdb/validation_reports/pa/1pam | 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 75230.086 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus sp. (bacteria) / Strain: 1011 / Description: ALKALOPHILIC BACILLUS SP. 1011 / Plasmid: PTUE254 / Production host: Escherichia coli (E. coli) / Strain (production host): ME8417 References: UniProt: P05618, cyclomaltodextrin glucanotransferase #2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 9 |
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-Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 49 % | ||||||||||||||||||||
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Crystal grow | pH: 5.6 Details: 1% PROTEIN, 20% PEG3000, 20% 2 PROPANOL,0.1M NA CITRATE, PH 5.6 | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS FR571 / Wavelength: 1.5418 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→29.6 Å / Num. obs: 111795 / % possible obs: 86.1 % / Observed criterion σ(I): 0 / Redundancy: 7 % / Rmerge(I) obs: 0.08 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: B. STEAROTHERMOPHILUS CGTASE Resolution: 1.8→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 22.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.83 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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