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- PDB-5i0d: Cycloalternan-forming enzyme from Listeria monocytogenes in compl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5i0d | |||||||||
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Title | Cycloalternan-forming enzyme from Listeria monocytogenes in complex with cycloalternan | |||||||||
![]() | Lmo2446 protein | |||||||||
![]() | SUGAR BINDING PROTEIN / Complex / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID | |||||||||
Function / homology | ![]() hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / carbohydrate metabolic process / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Light, S.H. / Minasov, G. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID) | |||||||||
![]() | ![]() Title: Transferase Versus Hydrolase: The Role of Conformational Flexibility in Reaction Specificity. Authors: Light, S.H. / Cahoon, L.A. / Mahasenan, K.V. / Lee, M. / Boggess, B. / Halavaty, A.S. / Mobashery, S. / Freitag, N.E. / Anderson, W.F. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 921.4 KB | Display | ![]() |
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PDB format | ![]() | 754.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 4.4 MB | Display | ![]() |
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Full document | ![]() | 4.4 MB | Display | |
Data in XML | ![]() | 99.6 KB | Display | |
Data in CIF | ![]() | 159.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5hopC ![]() 5hpoC ![]() 5hxmC ![]() 5i0eC ![]() 5i0fC ![]() 5i0gC ![]() 4kwuS S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Other databases |
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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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Components on special symmetry positions |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 120001.672 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC BAA-679 / EGD-e / Gene: lmo2446 / Production host: ![]() ![]() |
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-Sugars , 5 types, 13 molecules 
#2: Polysaccharide | alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source #3: Polysaccharide | Cyclic alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-3)-alpha-D- ...Cyclic alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose Source method: isolated from a genetically manipulated source #4: Polysaccharide | alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose | Source method: isolated from a genetically manipulated source #5: Polysaccharide | Cyclic alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-6)-alpha-D- ...Cyclic alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose | Source method: isolated from a genetically manipulated source #9: Sugar | |
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-Non-polymers , 4 types, 2830 molecules 






#6: Chemical | ChemComp-MG / #7: Chemical | #8: Chemical | ChemComp-CL / #10: Water | ChemComp-HOH / | |
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-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.79 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: Protein: 0.5 NaCl, 10 mM Tris pH 8.3, 5 mM BME Condition: 200 mM magnesium formate and 25% PEG 3350 Soak in mother liquor supplemented with 100 mM cycloalternan |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 21, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→30 Å / Num. obs: 233478 / % possible obs: 98.6 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.096 / Net I/σ(I): 14 |
Reflection shell | Resolution: 1.77→1.8 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.638 / Mean I/σ(I) obs: 2.1 / % possible all: 94.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4KWU Resolution: 1.77→30 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.961 / SU B: 4.039 / SU ML: 0.067 / Cross valid method: THROUGHOUT / ESU R: 0.099 / ESU R Free: 0.094 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.203 Å2
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Refinement step | Cycle: 1 / Resolution: 1.77→30 Å
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Refine LS restraints |
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