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Yorodumi- PDB-1wdp: The role of an inner loop in the catalytic mechanism of soybean b... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wdp | ||||||
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Title | The role of an inner loop in the catalytic mechanism of soybean beta-amylase | ||||||
Components | Beta-amylase | ||||||
Keywords | HYDROLASE / (beta/alpha)8 barrel | ||||||
Function / homology | Function and homology information beta-amylase / beta-amylase activity / amylopectin maltohydrolase activity / polysaccharide catabolic process Similarity search - Function | ||||||
Biological species | Glycine max (soybean) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / AB INITIO / Resolution: 1.27 Å | ||||||
Authors | Kang, Y.N. / Adachi, M. / Utsumi, S. / Mikami, B. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism. Authors: Kang, Y.N. / Tanabe, A. / Adachi, M. / Utsumi, S. / Mikami, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wdp.cif.gz | 245.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wdp.ent.gz | 197 KB | Display | PDB format |
PDBx/mmJSON format | 1wdp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wd/1wdp ftp://data.pdbj.org/pub/pdb/validation_reports/wd/1wdp | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | the biological assembly is a monomer |
-Components
#1: Protein | Mass: 55965.172 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Glycine max (soybean) / Plasmid: pKK233-2 / Production host: Escherichia coli (E. coli) / Strain (production host): JM105 / References: UniProt: P10538, beta-amylase | ||
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#2: Chemical | ChemComp-SO4 / #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: 1.98 Å3/Da / Density % sol: 37.8 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5.4 Details: ammonium sulfate, sodium acetate, 2-mercaptoethanol, EDTA, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.71 Å |
Detector | Type: RIGAKU RAXIS V / Detector: IMAGE PLATE / Date: Nov 29, 2003 |
Radiation | Monochromator: rotated-inclined double-crystal monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.71 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→50 Å / Num. all: 165296 / Num. obs: 163644 / % possible obs: 99 % / Observed criterion σ(I): 1 |
Reflection shell | Resolution: 1.25→1.29 Å / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: AB INITIO / Resolution: 1.27→10 Å / Num. parameters: 43836 / Num. restraintsaints: 52107 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze | Num. disordered residues: 11 / Occupancy sum hydrogen: 3825 / Occupancy sum non hydrogen: 4831 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.27→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.27→1.3 Å
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