+Open data
-Basic information
Entry | Database: PDB / ID: 2jey | ||||||
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Title | Mus musculus acetylcholinesterase in complex with HLo-7 | ||||||
Components | ACETYLCHOLINESTERASE | ||||||
Keywords | HYDROLASE / ACETYLCHOLINESTERASE / ALTERNATIVE SPLICING / OXIME / MOUSE / HLO-7 / SYNAPSE / MEMBRANE / NEUROTRANSMITTER DEGRADATION / MUS MUSCULUS / GLYCOPROTEIN / SERINE ESTERASE | ||||||
Function / homology | Function and homology information acetylcholine metabolic process / serine hydrolase activity / choline binding / acetylcholine catabolic process / acetylcholine binding / acetylcholinesterase / positive regulation of dendrite morphogenesis / acetylcholine receptor signaling pathway / choline metabolic process / osteoblast development ...acetylcholine metabolic process / serine hydrolase activity / choline binding / acetylcholine catabolic process / acetylcholine binding / acetylcholinesterase / positive regulation of dendrite morphogenesis / acetylcholine receptor signaling pathway / choline metabolic process / osteoblast development / acetylcholinesterase activity / positive regulation of axonogenesis / basement membrane / regulation of receptor recycling / synaptic cleft / side of membrane / laminin binding / collagen binding / synapse assembly / response to insulin / neuromuscular junction / receptor internalization / positive regulation of cold-induced thermogenesis / nuclear envelope / retina development in camera-type eye / presynaptic membrane / postsynaptic membrane / cell adhesion / endoplasmic reticulum lumen / axon / neuronal cell body / dendrite / synapse / perinuclear region of cytoplasm / Golgi apparatus / cell surface / protein homodimerization activity / extracellular space / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Ekstrom, F. / Astot, C. / Pang, Y.P. | ||||||
Citation | Journal: Clin.Pharmacol.Ther. / Year: 2007 Title: Novel Nerve-Agent Antidote Design Based on Crystallographic and Mass Spectrometric Analyses of Tabun-Conjugated Acetylcholinesterase in Complex with Antidotes. Authors: Ekstrom, F.J. / Astot, C. / Pang, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jey.cif.gz | 218.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jey.ent.gz | 175.2 KB | Display | PDB format |
PDBx/mmJSON format | 2jey.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jey_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 2jey_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 2jey_validation.xml.gz | 45.2 KB | Display | |
Data in CIF | 2jey_validation.cif.gz | 61.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/je/2jey ftp://data.pdbj.org/pub/pdb/validation_reports/je/2jey | HTTPS FTP |
-Related structure data
Related structure data | 2jezC 2jf0C 1j06S 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
#1: Protein | Mass: 60233.984 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 32-574 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PCDNA3.1 / Cell line (production host): HEK293 / Production host: HOMO SAPIENS (human) References: UniProt: P21836, acetylcholinesterase, carboxylesterase #2: Chemical | #3: Chemical | ChemComp-P6G / | #4: 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: 3.8 Å3/Da / Density % sol: 70 % |
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Crystal grow | pH: 7 / Details: 27-30 & PEG750MME, 0.1 M HEPES PH 7.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 1.082 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 29, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.082 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→29.88 Å / Num. obs: 51435 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 6.6 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 16 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 6.6 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 4.2 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1J06 Resolution: 2.7→29.88 Å / Cor.coef. Fo:Fc: 0.919 / Cor.coef. Fo:Fc free: 0.869 / SU B: 10.06 / SU ML: 0.207 / Cross valid method: THROUGHOUT / ESU R: 0.409 / ESU R Free: 0.293 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.75 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→29.88 Å
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