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- PDB-4m82: The structure of E292S glycosynthase variant of exo-1,3-beta-gluc... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4m82 | ||||||
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Title | The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans complexed with p-nitrophenyl-gentiobioside (product) at 1.6A resolution | ||||||
![]() | EXO-1,3-BETA-GLUCANASE | ||||||
![]() | HYDROLASE / TIM BARREL / GLYCOSIDE HYDROLASE FAMILY 5 / GLYCOSIDE HYDROLASE / CELL WALL HYDROLASE / GLYCOSYNTHASE / PROTEIN-CARBOHYDRATE INTERACTION | ||||||
Function / homology | ![]() glucan metabolic process / single-species biofilm formation in or on host organism / glucan 1,3-beta-glucosidase / glucan exo-1,3-beta-glucosidase activity / single-species biofilm formation on inanimate substrate / fungal-type cell wall organization / glucan catabolic process / Transferases; Glycosyltransferases; Hexosyltransferases / cell-substrate adhesion / cell adhesion molecule binding ...glucan metabolic process / single-species biofilm formation in or on host organism / glucan 1,3-beta-glucosidase / glucan exo-1,3-beta-glucosidase activity / single-species biofilm formation on inanimate substrate / fungal-type cell wall organization / glucan catabolic process / Transferases; Glycosyltransferases; Hexosyltransferases / cell-substrate adhesion / cell adhesion molecule binding / extracellular vesicle / transferase activity / cell surface / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nakatani, Y. / Cutfield, S.M. / Larsen, D.S. / Cutfield, J.F. | ||||||
![]() | ![]() Title: Major Change in Regiospecificity for the Exo-1,3-beta-glucanase from Candida albicans following Its Conversion to a Glycosynthase. Authors: Nakatani, Y. / Larsen, D.S. / Cutfield, S.M. / Cutfield, J.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 | ![]() | 107.7 KB | Display | ![]() |
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PDB format | ![]() | 79.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 725.2 KB | Display | ![]() |
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Full document | ![]() | 725.7 KB | Display | |
Data in XML | ![]() | 20.8 KB | Display | |
Data in CIF | ![]() | 32.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4m80C ![]() 4m81C ![]() 1cz1S 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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Unit cell |
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Components
#1: Protein | Mass: 45693.312 Da / Num. of mol.: 1 / Fragment: EXO-1,3-BETA-GLUCANASE (unp residues 40-438) / Mutation: E292S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: Q5AI63, UniProt: P29717*PLUS, glucan 1,3-beta-glucosidase | ||||
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#2: Sugar | ChemComp-NGB / | ||||
#3: Sugar | ChemComp-BGC / | ||||
#4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | DUE TO ALTERNATIVE CODON USAGE BY CANDIDA ALBICANS, THIS POSITION IS A SER WHEN FROM NATURAL ...DUE TO ALTERNATIV | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.09 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.3 Details: 0.1M HEPES-KOH, 0.2M CACL2, 19% PEG8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Nov 25, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.59→39.44 Å / Num. all: 48332 / Num. obs: 48285 / % possible obs: 99 % / Redundancy: 5.6 % / Biso Wilson estimate: 17.2 Å2 / Rmerge(I) obs: 0.027 / Rsym value: 0.027 / Net I/σ(I): 39.2 |
Reflection shell | Resolution: 1.59→1.68 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.212 / Mean I/σ(I) obs: 6.9 / Num. unique all: 6562 / Rsym value: 0.212 / % possible all: 93.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1CZ1 Resolution: 1.592→28.218 Å / SU ML: 0.14 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 16.67 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.592→28.218 Å
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Refine LS restraints |
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LS refinement shell |
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