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- PDB-1c2o: ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE -

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Basic information

Entry
Database: PDB / ID: 1c2o
TitleELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
ComponentsACETYLCHOLINESTERASE
KeywordsHYDROLASE / 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 / acetylcholine receptor signaling pathway / positive regulation of dendrite morphogenesis / osteoblast development / acetylcholinesterase activity ...acetylcholine metabolic process / serine hydrolase activity / choline binding / acetylcholine catabolic process / acetylcholine binding / acetylcholinesterase / acetylcholine receptor signaling pathway / positive regulation of dendrite morphogenesis / osteoblast development / acetylcholinesterase activity / choline metabolic process / positive regulation of axonogenesis / basement membrane / regulation of receptor recycling / side of membrane / synaptic cleft / laminin binding / synapse assembly / collagen binding / response to insulin / neuromuscular junction / receptor internalization / : / retina development in camera-type eye / nuclear envelope / 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 / Golgi apparatus / cell surface / protein homodimerization activity / extracellular space / identical protein binding / plasma membrane
Similarity search - Function
Acetylcholinesterase, tetramerisation domain / Acetylcholinesterase tetramerisation domain / Cholinesterase / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase type B, active site / Carboxylesterases type-B serine active site. / Carboxylesterase, type B / Carboxylesterase family / Alpha/Beta hydrolase fold
Similarity search - Domain/homology
Acetylcholinesterase
Similarity search - Component
Biological speciesElectrophorus electricus (electric eel)
MethodX-RAY DIFFRACTION / Resolution: 4.2 Å
AuthorsBourne, Y. / Marchot, P.
CitationJournal: 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
DepositionJul 26, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 19, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 21, 2014Group: Other
Revision 1.4Jun 2, 2021Group: Derived calculations
Category: pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ACETYLCHOLINESTERASE
B: ACETYLCHOLINESTERASE
C: ACETYLCHOLINESTERASE
D: ACETYLCHOLINESTERASE


Theoretical massNumber of molelcules
Total (without water)237,1684
Polymers237,1684
Non-polymers00
Water00
1
A: ACETYLCHOLINESTERASE
D: ACETYLCHOLINESTERASE


Theoretical massNumber of molelcules
Total (without water)118,5842
Polymers118,5842
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1780 Å2
ΔGint-14 kcal/mol
Surface area37350 Å2
MethodPISA
2
B: ACETYLCHOLINESTERASE
C: ACETYLCHOLINESTERASE


Theoretical massNumber of molelcules
Total (without water)118,5842
Polymers118,5842
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1790 Å2
ΔGint-14 kcal/mol
Surface area37330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)211.160, 129.750, 195.420
Angle α, β, γ (deg.)90.00, 103.20, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
ACETYLCHOLINESTERASE


Mass: 59292.012 Da / Num. of mol.: 4 / Fragment: A4 FORM / Source method: isolated from a natural source / Details: ELECTRIC ORGAN / Source: (natural) Electrophorus electricus (electric eel) / References: UniProt: P21836, acetylcholinesterase
Source detailsTHE SEQUENCE LISTED IN THE SEQRES RECORD IS OF MOUSE ACETYLCHOLINESTERASE, (CORRESPONDING TO THE ...THE SEQUENCE LISTED IN THE SEQRES RECORD IS OF MOUSE ACETYLCHOLINESTERASE, (CORRESPONDING TO THE STRUCTURE) NOT OF ELECTROPHORUS ELECTRICUS. AT THE RESOLUTION OF THE EXPERIMENTAL DATA (4.2A) NO SEQUENCE DISCREPANCIES CAN BE SEEN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 5.49 Å3/Da / Density % sol: 77.61 %
Crystal growTemperature: 298 K / Method: vapor diffusion / pH: 5.5
Details: 1.4 M ammonium sulfate, VAPOR DIFFUSION, temperature 298K, pH 5.5
Crystal
*PLUS
Density % sol: 69.5 %
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

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 15, 1996
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 4.2→12 Å / Num. obs: 24590 / % possible obs: 66 % / Redundancy: 1.9 % / Rmerge(I) obs: 0.18
Reflection
*PLUS
Num. measured all: 158367

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALAdata scaling
AMoREphasing
CNSrefinement
CCP4(SCALA)data scaling
RefinementResolution: 4.2→12 Å
RfactorNum. reflection% reflection
Rfree0.385 --
Rwork0.375 --
obs-24590 66 %
Refinement stepCycle: LAST / Resolution: 4.2→12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16688 0 0 0 16688
Software
*PLUS
Name: 'CNS' / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDType
X-RAY DIFFRACTIONc_bond_d
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_deg
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scangle_it

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