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- PDB-2jkp: Structure of a family 97 alpha-glucosidase from Bacteroides theta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2jkp | ||||||
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Title | Structure of a family 97 alpha-glucosidase from Bacteroides thetaiotaomicron in complex with castanospermine | ||||||
![]() | ALPHA-GLUCOSIDASE (ALPHA-GLUCOSIDASE SUSB) | ||||||
![]() | HYDROLASE / FAMILY 97 / CASTANOSPERMINE / ALPHA-GLUCOSIDASE / GLYCOSIDE HYDROLASE / BACTEROIDES THETAIOTAOMICRON | ||||||
Function / homology | ![]() glucan 1,4-alpha-glucosidase / alpha-1,4-glucosidase activity / glucan 1,4-alpha-glucosidase activity / starch catabolic process / carbohydrate binding / periplasmic space / calcium ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gloster, T.M. / Turkenburg, J.P. / Potts, J.R. / Henrissat, B. / Davies, G.J. | ||||||
![]() | ![]() Title: Divergence of Catalytic Mechanism within a Glycosidase Family Provides Insight Into Evolution of Carbohydrate Metabolism by Human Gut Flora. Authors: Gloster, T.M. / Turkenburg, J.P. / Potts, J.R. / Henrissat, B. / Davies, G.J. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 314.6 KB | Display | ![]() |
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PDB format | ![]() | 251.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 469.8 KB | Display | ![]() |
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Full document | ![]() | 486.9 KB | Display | |
Data in XML | ![]() | 63 KB | Display | |
Data in CIF | ![]() | 94.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2jkaSC ![]() 2jkeC 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 83307.289 Da / Num. of mol.: 2 / Fragment: RESIDUES 22-738 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: VPI-5482 / Production host: ![]() ![]() References: UniProt: P71094, UniProt: G8JZS4*PLUS, alpha-glucosidase #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-EDO / #5: Water | ChemComp-HOH / | Sequence details | THE FIRST 21 RESIDUES OF THE GENE CORRESPOND TO A SIGNAL PEPTIDE SEQUENCE AND WERE NOT CLONED INTO ...THE FIRST 21 RESIDUES OF THE GENE CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 58 % / Description: STRUCTURE ISOMORPHOUS WITH STARTING MODEL |
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Crystal grow | Details: 18-22% POLYETHYLENE GLYCOL 3350 AND 0.02 M SODIUM/POTASSIUM PHOSPHATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 23, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 108971 / % possible obs: 95.3 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 13.3 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 2.2 / % possible all: 69.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2JKA Resolution: 1.99→102.06 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.939 / SU B: 4.329 / SU ML: 0.118 / Cross valid method: THROUGHOUT / ESU R: 0.172 / ESU R Free: 0.163 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.07 Å2
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Refinement step | Cycle: LAST / Resolution: 1.99→102.06 Å
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Refine LS restraints |
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