+Open data
-Basic information
Entry | Database: PDB / ID: 1vff | ||||||
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Title | beta-glycosidase from Pyrococcus horikoshii | ||||||
Components | beta-glucosidase | ||||||
Keywords | HYDROLASE / glycosyl hydrolase / membrane-bound enzyme / thermostability / TIM barrel / alkylglucosides | ||||||
Function / homology | Function and homology information hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate metabolic process Similarity search - Function | ||||||
Biological species | Pyrococcus horikoshii (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Akiba, T. / Nishio, M. / Matsui, I. / Harata, K. | ||||||
Citation | Journal: Proteins / Year: 2004 Title: X-ray structure of a membrane-bound beta-glycosidase from the hyperthermophilic archaeon Pyrococcus horikoshii Authors: Akiba, T. / Nishio, M. / Matsui, I. / Harata, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vff.cif.gz | 99.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vff.ent.gz | 76.5 KB | Display | PDB format |
PDBx/mmJSON format | 1vff.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vf/1vff ftp://data.pdbj.org/pub/pdb/validation_reports/vf/1vff | HTTPS FTP |
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-Related structure data
Related structure data | 1gowS S: Starting model for refinement |
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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
#1: Protein | Mass: 50400.859 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Gene: PH0366 / Plasmid: pET11a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O58104, beta-glucosidase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.8 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: lithium sulfate, sodium acetate, Triton X-100, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 0.977 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 1, 2001 / Details: bent fused quartz mirror |
Radiation | Monochromator: bent Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.977 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→28.7 Å / Num. all: 18851 / Num. obs: 18851 / % possible obs: 98.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 29.4 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 17.5 |
Reflection shell | Resolution: 2.5→2.65 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.273 / Mean I/σ(I) obs: 4.1 / Num. unique all: 2729 / % possible all: 98.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GOW Resolution: 2.5→9.97 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 1699679.57 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 56.8819 Å2 / ksol: 0.408794 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→9.97 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.65 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
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Xplor file |
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