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Yorodumi- PDB-1tux: HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE XYLANASE FROM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tux | ||||||
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Title | HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE XYLANASE FROM THERMOASCUS AURANTIACUS | ||||||
Components | XYLANASE | ||||||
Keywords | HYDROLASE / XYLAN DEGRADATION / GLYCOSIDASE / ENZYME / 1 / 4-BETA-XYLAN XYLANOHYDROLASE | ||||||
Function / homology | Function and homology information endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process Similarity search - Function | ||||||
Biological species | Thermoascus aurantiacus (fungus) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Natesh, R. / Bhanumoorthy, P. / Vithayathil, P.J. / Sekar, K. / Ramakumar, S. / Viswamitra, M.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: Crystal structure at 1.8 A resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus. Authors: Natesh, R. / Bhanumoorthy, P. / Vithayathil, P.J. / Sekar, K. / Ramakumar, S. / Viswamitra, M.A. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization and Preliminary X-Ray Diffraction Analysis of Crystals of Thermoascus Aurantiacus Xylanase Authors: Viswamitra, M.A. / Bhanumoorthy, P. / Ramakumar, S. / Manjula, M.V. / Vithayathil, P.J. / Murthy, S.K. / Naren, A.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tux.cif.gz | 74.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tux.ent.gz | 54.5 KB | Display | PDB format |
PDBx/mmJSON format | 1tux.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tu/1tux ftp://data.pdbj.org/pub/pdb/validation_reports/tu/1tux | 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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-Components
#1: Protein | Mass: 32556.385 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: FUNGAL SOURCE FROM THERMOASCUS AURANTIACUS XYLANASE Source: (natural) Thermoascus aurantiacus (fungus) / Strain: LOCAL INDIAN SOIL / References: UniProt: P23360, endo-1,4-beta-xylanase |
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#2: Water | ChemComp-HOH / |
Sequence details | THE SEQUENCE DEPOSITED IN THE SEQRES RECORDS IS IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 42 % Description: THE FULL ATOMIC COORDINATES OF THE WILD TYPE STREPTOMYCES LIVIDANS XYLANASE KINDLY PROVIDED TO US BY PROF. Z. DEREWENDA WERE USED AS THE STARTING MODEL FOR MOLECULAR REPLACEMENT. ONLY CA ...Description: THE FULL ATOMIC COORDINATES OF THE WILD TYPE STREPTOMYCES LIVIDANS XYLANASE KINDLY PROVIDED TO US BY PROF. Z. DEREWENDA WERE USED AS THE STARTING MODEL FOR MOLECULAR REPLACEMENT. ONLY CA COORDINATES OF STREPTOMYCES LIVIDANS XYLANASE ARE DEPOSITED IN PDB WITH ID CODE 1XAS TILL DATE. STRUCTURE REFINEMENT USING HIGH RESOLUTION DATA SETS AT 1.11 AND 0.89 A COLLECTED AT DIFFERENT TEMPERATURES IS CURRENTLY | ||||||||||||||||||||
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Crystal grow | pH: 7.2 / Details: pH 7.2 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
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: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 5, 1997 |
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→99 Å / Num. obs: 22983 / % possible obs: 93 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.05 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.11 / % possible all: 86.1 |
Reflection | *PLUS Num. measured all: 85248 |
Reflection shell | *PLUS % possible obs: 86.1 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: STREPTOMYCES LIVIDANS XYLANASE Resolution: 1.8→10 Å / Rfactor Rfree error: 0.21 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
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Refine analyze |
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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→1.86 Å / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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