+Open data
-Basic information
Entry | Database: PDB / ID: 2c0q | ||||||
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Title | non-aged form of mouse acetylcholinesterase inhibited by tabun | ||||||
Components | ACETYLCHOLINESTERASE | ||||||
Keywords | HYDROLASE / SERINE ESTERASE / ACETYLCHOLINESTERASE | ||||||
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: 2.5 Å | ||||||
Authors | Ekstrom, F. / Akfur, C. / Tunemalm, A.-K. / Lundberg, S. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Structural Changes of Phenylalanine 338 and Histidine 447 Revealed by the Crystal Structures of Tabun-Inhibited Murine Acetylcholinesterase. Authors: Ekstrom, F. / Akfur, C. / Tunemalm, A.-K. / Lundberg, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2c0q.cif.gz | 219.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2c0q.ent.gz | 175.4 KB | Display | PDB format |
PDBx/mmJSON format | 2c0q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2c0q_validation.pdf.gz | 735 KB | Display | wwPDB validaton report |
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Full document | 2c0q_full_validation.pdf.gz | 750.4 KB | Display | |
Data in XML | 2c0q_validation.xml.gz | 40.9 KB | Display | |
Data in CIF | 2c0q_validation.cif.gz | 57.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c0/2c0q ftp://data.pdbj.org/pub/pdb/validation_reports/c0/2c0q | HTTPS FTP |
-Related structure data
Related structure data | 2c0pC 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 Details: TABUN REACTION PRODUCT COVALENTLY ATTACHED TO SER203 Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PCDNA3.1 / Cell line (production host): HEK293F / Production host: HOMO SAPIENS (human) / References: UniProt: P21836, acetylcholinesterase #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: 27-31% (V/V) PEG750MME, 0.1M 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: 1.06276 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 8, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.06276 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→29.2 Å / Num. obs: 71021 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 6.2 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.59 / Mean I/σ(I) obs: 3.3 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1J06 Resolution: 2.5→29.17 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.915 / SU B: 7.272 / SU ML: 0.158 / Cross valid method: THROUGHOUT / ESU R: 0.245 / ESU R Free: 0.218 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Displacement parameters | Biso mean: 47.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→29.17 Å
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Refine LS restraints |
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