+Open data
-Basic information
Entry | Database: PDB / ID: 2d05 | ||||||
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Title | Chitosanase From Bacillus circulans mutant K218P | ||||||
Components | Chitosanase | ||||||
Keywords | HYDROLASE / CHITOSAN DEGRADATION | ||||||
Function / homology | Function and homology information chitosanase / chitosanase activity / carbohydrate metabolic process / extracellular region Similarity search - Function | ||||||
Biological species | Bacillus circulans (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Fukamizo, T. / Amano, S. / Yamaguchi, K. / Yoshikawa, T. / Katsumi, T. / Saito, J. / Suzuki, M. / Miki, K. / Nagata, Y. / Ando, A. | ||||||
Citation | Journal: J.Biochem.(Tokyo) / Year: 2005 Title: Bacillus circulans MH-K1 Chitosanase: Amino Acid Residues Responsible for Substrate Binding Authors: Fukamizo, T. / Amano, S. / Yamaguchi, K. / Yoshikawa, T. / Katsumi, T. / Saito, J. / Suzuki, M. / Miki, K. / Nagata, Y. / Ando, A. #1: Journal: J.Biol.Chem. / Year: 1999 Title: Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism Authors: Saito, J. / Kita, A. / Higuchi, Y. / Nagata, Y. / Ando, A. / Miki, K. #2: Journal: ACTA CRYSTALLOGR.,SECT.D / Year: 1995 Title: Crystallization and preliminary X-ray crystallographic analysis of chitosanase from Bacillus circulans MH-K1 Authors: Saito, J.I. / Nagata, Y. / Ando, A. / Kita, A. / Miki, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2d05.cif.gz | 63 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2d05.ent.gz | 49.2 KB | Display | PDB format |
PDBx/mmJSON format | 2d05.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d0/2d05 ftp://data.pdbj.org/pub/pdb/validation_reports/d0/2d05 | HTTPS FTP |
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-Related structure data
Related structure data | |
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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 on special symmetry positions |
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-Components
#1: Protein | Mass: 28955.352 Da / Num. of mol.: 1 / Mutation: K218P Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus circulans (bacteria) / Strain: MH-K1 / Production host: Brevibacillus choshinensis (bacteria) / Strain (production host): HPD31 / References: UniProt: P33673, chitosanase |
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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: 2.77 Å3/Da / Density % sol: 55.55 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: Ammonium sulfate, Tris-HCl, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→100 Å / Num. all: 19983 / Num. obs: 19983 / % possible obs: 88.5 % / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2→2.07 Å / % possible all: 79.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→40 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→40 Å
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