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- PDB-2bs9: Native crystal structure of a GH39 beta-xylosidase XynB1 from Geo... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bs9 | ||||||
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Title | Native crystal structure of a GH39 beta-xylosidase XynB1 from Geobacillus stearothermophilus | ||||||
![]() | BETA-XYLOSIDASE | ||||||
![]() | HYDROLASE / BETA-XYLOSIDASE / COMPLEX OF THE COVALENT INTERMEDIATE / ENZYME-SUBSTRATE COMPLEX / FAMILY GH39 / THERMOPHILIC ENZYME | ||||||
Function / homology | ![]() xylan 1,4-beta-xylosidase / xylan 1,4-beta-xylosidase activity / xylan catabolic process Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Czjzek, M. / Bravman, T. / Henrissat, B. / Shoham, Y. | ||||||
![]() | ![]() Title: Enzyme-Substrate Complex Structures of a Gh39 Beta-Xylosidase from Geobacillus Stearothermophilus. Authors: Czjzek, M. / David, A.B. / Bravman, T. / Shoham, G. / Henrissat, B. / Shoham, Y. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: Crystallization and Preliminary X-Ray Analysis of Family 39 Beta-D-Xylosidase from Geobacillus Stearothermophilus T-6 Authors: Czjzek, M. / Bravman, T. / Henrissat, B. / Shoham, Y. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB BB CB" IN EACH CHAIN ON SHEET RECORDS ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB BB CB" IN EACH CHAIN ON SHEET RECORDS BELOW ARE ACTUALLY 8-STRANDED BARRELS REPRESENTED BY 9-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "DB EB FB GB HB" IN EACH CHAIN ON SHEET RECORDS BELOW ARE ACTUALLY 7-STRANDED BARRELS REPRESENTED BY 8-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 806.1 KB | Display | ![]() |
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PDB format | ![]() | 670.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 507.7 KB | Display | ![]() |
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Full document | ![]() | 579.6 KB | Display | |
Data in XML | ![]() | 149.3 KB | Display | |
Data in CIF | ![]() | 207.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bfgC ![]() 1px8S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: SER / End label comp-ID: SER / Refine code: 5 / Auth seq-ID: 2 - 502 / Label seq-ID: 2 - 502
NCS oper:
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Components
#1: Protein | Mass: 58058.824 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52 % |
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Crystal grow | pH: 7.5 Details: 100 MM HEPES PH 7.5, 50 MM NACL, 20% (W/V) PEG 8000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jun 25, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→24.9 Å / Num. obs: 273112 / % possible obs: 98.2 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.16 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.1→2.2 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 2.4 / % possible all: 98.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1PX8 Resolution: 2.2→50 Å / Cor.coef. Fo:Fc: 0.913 / Cor.coef. Fo:Fc free: 0.875 / SU B: 5.067 / SU ML: 0.127 / Cross valid method: THROUGHOUT / ESU R: 0.29 / ESU R Free: 0.227 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.34 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→50 Å
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Refine LS restraints |
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