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- PDB-1uz1: Family 1 b-glucosidase from Thermotoga maritima in complex with i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1uz1 | ||||||
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Title | Family 1 b-glucosidase from Thermotoga maritima in complex with isofagomine lactam | ||||||
![]() | BETA-GLUCOSIDASE A | ||||||
![]() | HYDROLASE / GLUCOSIDE HYDROLYSIS / FAMILY GH1 / ENZYME / ISOFAGOMINE LACTAM | ||||||
Function / homology | ![]() scopolin beta-glucosidase activity / beta-glucosidase / beta-glucosidase activity / cellulose catabolic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gloster, T.M. / Macdonald, J. / Stick, R.V. / Davies, G.J. | ||||||
![]() | ![]() Title: Common Inhibition of Both -Glucosidases and -Mannosidases by Isofagomine Lactam Reflects Different Conformational Itineraries for Pyranoside Hydrolysis Authors: Vincent, F. / Gloster, T.M. / Macdonald, J. / Morland, C. / Stick, R.V. / Dias, F.M.V. / Prates, J.A.M. / Fontes, C.M.G.A. / Gilbert, H.J. / Davies, G.J. #1: ![]() Title: Glycosidase Inhibition: An Assessment of the Binding of 18 Putative Transition-State Mimics. Authors: Gloster, T.M. / Meloncelli, P. / Stick, R.V. / Zechel, D. / Vasella, A. / Davies, G.J. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" AND "BB" IN EACH CHAIN ON SHEET ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" AND "BB" IN EACH CHAIN ON SHEET RECORDS BELOW ARE ACTUALLY 8-STRANDED BARRELS THAT ARE REPRESENTED BY 9-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 | ![]() | 200.7 KB | Display | ![]() |
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PDB format | ![]() | 158.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 454.1 KB | Display | ![]() |
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Full document | ![]() | 462.8 KB | Display | |
Data in XML | ![]() | 38 KB | Display | |
Data in CIF | ![]() | 55.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1uz4C ![]() 1od0S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.02078, -0.99212, -0.12358), Vector: |
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Components
#1: Protein | Mass: 53940.648 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: CATALYTIC MODULE / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THE FULL LENGTH PROTEIN ALSO CONTAINS A HIS-TAG FROM THE PET28A CLONING VECTOR. NUMBERING OF THE ...THE FULL LENGTH PROTEIN ALSO CONTAINS A HIS-TAG FROM THE PET28A CLONING VECTOR. NUMBERING OF THE PROTEIN AGREES WITH THE UNIPROT ENTRY AND THUS IGNORES THE HIS-TAG. ANY MISSING RESIDUES/ATOMS ARE DUE TO POOR OR A LACK OF ELECTRON DENSITY | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46 % / Description: STRUCTURE ISOMORPHOUS WITH STARTING MODEL |
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Crystal grow | pH: 7 Details: 10MG/ML PROTEIN IN 15% PEG 4000, 0.2 M CAAC, 0.1 M IMIDAZOLE PH7, pH 7.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Dec 15, 2002 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: DOUBLE CRYSTAL, SI(111) OR SI(311) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.065 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 65765 / % possible obs: 96 % / Redundancy: 4.95 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 24.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.73 % / Rmerge(I) obs: 0.437 / Mean I/σ(I) obs: 2.34 / % possible all: 84.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1OD0 Resolution: 2→72.55 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.933 / SU B: 4.608 / SU ML: 0.129 / Cross valid method: THROUGHOUT / ESU R: 0.2 / ESU R Free: 0.178 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.04 Å2
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Refinement step | Cycle: LAST / Resolution: 2→72.55 Å
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Refine LS restraints |
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