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Yorodumi- PDB-5nap: Torpedo californica acetylcholinesterase in complex with a non-ch... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5nap | |||||||||
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Title | Torpedo californica acetylcholinesterase in complex with a non-chiral donepezil-like inhibitor 17 | |||||||||
Components | Acetylcholinesterase | |||||||||
Keywords | HYDROLASE / Acetylcholinesterase / inhibitors / Alzheimer's disease / donepezil analogues / green chemistry | |||||||||
Function / homology | Function and homology information acetylcholine catabolic process in synaptic cleft / acetylcholinesterase / acetylcholinesterase activity / synaptic cleft / side of membrane / synapse / plasma membrane Similarity search - Function | |||||||||
Biological species | Tetronarce californica (Pacific electric ray) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.17 Å | |||||||||
Authors | Caliandro, R. / Pesaresi, A. / Lamba, D. | |||||||||
Citation | Journal: J Enzyme Inhib Med Chem / Year: 2018 Title: Kinetic and structural studies on the interactions of Torpedo californica acetylcholinesterase with two donepezil-like rigid analogues. Authors: Caliandro, R. / Pesaresi, A. / Cariati, L. / Procopio, A. / Oliverio, M. / Lamba, D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5nap.cif.gz | 133.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5nap.ent.gz | 102.9 KB | Display | PDB format |
PDBx/mmJSON format | 5nap.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/na/5nap ftp://data.pdbj.org/pub/pdb/validation_reports/na/5nap | HTTPS FTP |
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-Related structure data
Related structure data | 5nauC 5e4tS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 61325.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Tetronarce californica (Pacific electric ray) References: UniProt: P04058, acetylcholinesterase | ||||
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#2: Polysaccharide | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Chemical | ChemComp-DZ7 / ( | #5: 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: 4.01 Å3/Da / Density % sol: 69.31 % |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, hanging drop / Details: MES 100 mM, pH 6.2 PEG 200 30% |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ELETTRA / Beamline: 5.2R / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jul 10, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→78.92 Å / Num. obs: 52442 / % possible obs: 100 % / Redundancy: 5.9 % / Rmerge(I) obs: 0.119 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2.17→2.29 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.526 / Mean I/σ(I) obs: 3.1 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5E4T Resolution: 2.17→55.9 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.943 / SU B: 3.489 / SU ML: 0.092 / Cross valid method: THROUGHOUT / ESU R: 0.149 / ESU R Free: 0.144 / 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: 30.66 Å2
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Refinement step | Cycle: LAST / Resolution: 2.17→55.9 Å
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Refine LS restraints |
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