+Open data
-Basic information
Entry | Database: PDB / ID: 5ch3 | ||||||
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Title | E3 alpha-esterase-7 carboxylesterase | ||||||
Components | Carboxylic ester hydrolaseCarboxylesterase | ||||||
Keywords | HYDROLASE / Carboxylesterase / OP hydrolase / organophosphates / structural dynamics | ||||||
Function / homology | Function and homology information Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases / carboxylic ester hydrolase activity Similarity search - Function | ||||||
Biological species | Lucilia cuprina (Australian sheep blowfly) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.71 Å | ||||||
Authors | Correy, G. / Mabbitt, P. / Jackson, C.J. | ||||||
Citation | Journal: Structure / Year: 2016 Title: Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic Crystallography. Authors: Correy, G.J. / Carr, P.D. / Meirelles, T. / Mabbitt, P.D. / Fraser, N.J. / Weik, M. / Jackson, C.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ch3.cif.gz | 133.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ch3.ent.gz | 101.3 KB | Display | PDB format |
PDBx/mmJSON format | 5ch3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ch/5ch3 ftp://data.pdbj.org/pub/pdb/validation_reports/ch/5ch3 | HTTPS FTP |
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-Related structure data
Related structure data | 4qwmC 4ubiC 4ubjC 4ubkC 4ublC 4ubmC 4ubnC 4uboC 4w1pC 4w1qC 4w1rC 4w1sC 5ch5C 5ivdC 5ivhC 5iviC 5ivkC 4fngS C: citing same article (ref.) 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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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 66388.836 Da / Num. of mol.: 1 / Mutation: D83A, M364L, I419F, A472T, I505T, K530E, D554G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lucilia cuprina (Australian sheep blowfly) Gene: LcaE7 / Production host: Escherichia coli (E. coli) References: UniProt: Q25252, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.46 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: 20% PEG 2K MME, 100mM sodium acetate pH 4.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9393 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 20, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9393 Å / Relative weight: 1 |
Reflection | Resolution: 1.71→45.8 Å / Num. obs: 56138 / % possible obs: 99.9 % / Redundancy: 29 % / Rmerge(I) obs: 0.145 / Net I/σ(I): 19.5 |
Reflection shell | Resolution: 1.71→1.74 Å / Redundancy: 28.3 % / Rmerge(I) obs: 3.8 / Mean I/σ(I) obs: 1.1 / % possible all: 98.6 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4FNG Resolution: 1.71→45.76 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.958 / SU B: 3.725 / SU ML: 0.109 / Cross valid method: THROUGHOUT / ESU R: 0.108 / ESU R Free: 0.11 / 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: 34.233 Å2
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Refinement step | Cycle: LAST / Resolution: 1.71→45.76 Å
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Refine LS restraints |
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