+Open data
-Basic information
Entry | Database: PDB / ID: 1c2b | ||||||
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Title | ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE | ||||||
Components | ACETYLCHOLINESTERASE | ||||||
Keywords | HYDROLASE / SERINE HYDROLASE / ALPHA/BETA HYDROLASE / TETRAMER | ||||||
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 / side of membrane / synaptic cleft / laminin binding / collagen binding / synapse assembly / response to insulin / neuromuscular junction / receptor internalization / nuclear envelope / retina development in camera-type eye / presynaptic membrane / positive regulation of cold-induced thermogenesis / postsynaptic membrane / cell adhesion / endoplasmic reticulum lumen / axon / neuronal cell body / synapse / dendrite / perinuclear region of cytoplasm / cell surface / Golgi apparatus / protein homodimerization activity / extracellular space / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Electrophorus electricus (electric eel) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 4.5 Å | ||||||
Authors | Bourne, Y. / Marchot, P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1999 Title: Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography. Authors: Bourne, Y. / Grassi, J. / Bougis, P.E. / Marchot, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c2b.cif.gz | 98.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c2b.ent.gz | 78.1 KB | Display | PDB format |
PDBx/mmJSON format | 1c2b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1c2b_validation.pdf.gz | 368.4 KB | Display | wwPDB validaton report |
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Full document | 1c2b_full_validation.pdf.gz | 400.4 KB | Display | |
Data in XML | 1c2b_validation.xml.gz | 15.9 KB | Display | |
Data in CIF | 1c2b_validation.cif.gz | 23 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c2/1c2b ftp://data.pdbj.org/pub/pdb/validation_reports/c2/1c2b | HTTPS FTP |
-Related 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: 59421.129 Da / Num. of mol.: 1 / Fragment: A4 FORM / Source method: isolated from a natural source / Details: A4 FORM / Source: (natural) Electrophorus electricus (electric eel) / References: UniProt: P21836, acetylcholinesterase |
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Source details | THE SEQUENCE LISTED IN THE SEQRES RECORD IS OF MOUSE ACETYLCHOLINESTERASE, (CORRESPONDING TO THE ...THE SEQUENCE LISTED IN THE SEQRES RECORD IS OF MOUSE ACETYLCHOL |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 6.15 Å3/Da / Density % sol: 79.99 % |
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Crystal grow | Temperature: 279 K / Method: vapor diffusion / pH: 8 / Details: NaKPO4, VAPOR DIFFUSION, pH 8.0, temperature 279K |
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / PH range low: 6 / PH range high: 5.5 |
Components of the solutions | *PLUS Conc.: 1.4 M / Common name: ammonium sulfate |
-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 15, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 4.5→10 Å / Num. obs: 7742 / % possible obs: 74 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.2 |
Reflection | *PLUS Num. measured all: 101833 / Rmerge(I) obs: 0.2 |
-Processing
Software |
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Refinement | Resolution: 4.5→10 Å /
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Refinement step | Cycle: LAST / Resolution: 4.5→10 Å
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||
Refinement | *PLUS Highest resolution: 4.5 Å / Lowest resolution: 10 Å / Rfactor obs: 0.369 | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS |