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Yorodumi- PDB-6qaa: Human Butyrylcholinesterase in complex with (S)-2-(butylamino)-N-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6qaa | |||||||||
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Title | Human Butyrylcholinesterase in complex with (S)-2-(butylamino)-N-(2-cycloheptylethyl)-3-(1H-indol-3-yl)propanamide | |||||||||
Components | Cholinesterase | |||||||||
Keywords | HYDROLASE / Butyrylcholinesterase / inhibitor / complex | |||||||||
Function / homology | Function and homology information cholinesterase / cocaine metabolic process / neuroblast differentiation / Neurotransmitter clearance / cholinesterase activity / choline binding / response to folic acid / response to alkaloid / acetylcholine catabolic process / negative regulation of synaptic transmission ...cholinesterase / cocaine metabolic process / neuroblast differentiation / Neurotransmitter clearance / cholinesterase activity / choline binding / response to folic acid / response to alkaloid / acetylcholine catabolic process / negative regulation of synaptic transmission / peptide hormone processing / acetylcholinesterase activity / choline metabolic process / hydrolase activity, acting on ester bonds / Aspirin ADME / nuclear envelope lumen / Synthesis of PC / Synthesis, secretion, and deacylation of Ghrelin / catalytic activity / response to glucocorticoid / xenobiotic metabolic process / learning / amyloid-beta binding / blood microparticle / negative regulation of cell population proliferation / endoplasmic reticulum lumen / enzyme binding / extracellular space / extracellular region / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.897 Å | |||||||||
Authors | Brazzolotto, X. / Nachon, F. / Harst, M. / Knez, D. / Gobec, S. | |||||||||
Funding support | France, 1items
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Citation | Journal: Chem.Commun.(Camb.) / Year: 2019 Title: Tryptophan-derived butyrylcholinesterase inhibitors as promising leads against Alzheimer's disease. Authors: Meden, A. / Knez, D. / Jukic, M. / Brazzolotto, X. / Grsic, M. / Pislar, A. / Zahirovic, A. / Kos, J. / Nachon, F. / Svete, J. / Gobec, S. / Groselj, U. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6qaa.cif.gz | 137.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6qaa.ent.gz | 102.1 KB | Display | PDB format |
PDBx/mmJSON format | 6qaa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qa/6qaa ftp://data.pdbj.org/pub/pdb/validation_reports/qa/6qaa | HTTPS FTP |
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-Related structure data
Related structure data | 6qabC 6qacC 6qadC 6qaeC 1poiS 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 63029.668 Da / Num. of mol.: 1 / Mutation: N45Q, N483Q, N509Q, N514Q, 558STOP Source method: isolated from a genetically manipulated source Details: Residues 1 to 28 are signal peptide / Source: (gene. exp.) Homo sapiens (human) / Gene: BCHE, CHE1 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P06276, cholinesterase |
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-Sugars , 3 types, 6 molecules
#2: Polysaccharide | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||
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#3: Polysaccharide | #4: Sugar | |
-Non-polymers , 6 types, 298 molecules
#5: Chemical | #6: Chemical | ChemComp-HUN / | #7: Chemical | ChemComp-GOL / #8: Chemical | ChemComp-MES / | #9: Chemical | ChemComp-SO4 / #10: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.56 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: Ammonium Sulfate MES pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9724 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 19, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9724 Å / Relative weight: 1 |
Reflection | Resolution: 1.897→48.89 Å / Num. obs: 61234 / % possible obs: 99.9 % / Redundancy: 8.7 % / Biso Wilson estimate: 31.56 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.07043 / Rpim(I) all: 0.02501 / Rrim(I) all: 0.07489 / Net I/σ(I): 17.96 |
Reflection shell | Resolution: 1.897→1.965 Å / Redundancy: 8.5 % / Rmerge(I) obs: 0.8126 / Mean I/σ(I) obs: 2.54 / Num. unique obs: 6026 / CC1/2: 0.797 / Rpim(I) all: 0.2939 / Rrim(I) all: 0.8659 / % possible all: 99.93 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1POI Resolution: 1.897→48.888 Å / SU ML: 0.2 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.97 / 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: 1.897→48.888 Å
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Refine LS restraints |
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LS refinement shell |
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