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- PDB-1amn: TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH M-(N... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1amn | ||||||
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Title | TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE | ||||||
![]() | ACETYLCHOLINESTERASE | ||||||
![]() | HYDROLASE (SERINE ESTERASE) / HYDROLASE / SERINE ESTERASE / SYNAPSE / MEMBRANE / NERVE / MUSCLE / NEUROTRANSMITTER DEGRADATION / GLYCOPROTEIN / GPI-ANCHOR / ALTERNATIVE SPLICING | ||||||
Function / homology | ![]() acetylcholine catabolic process in synaptic cleft / acetylcholinesterase / acetylcholinesterase activity / choline metabolic process / side of membrane / synaptic cleft / synapse / extracellular space / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Harel, M. / Silman, I. / Sussman, J.L. | ||||||
![]() | Journal: J.Am.Chem.Soc. / Year: 1996 Title: The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. Authors: Harel, M. / Quinn, D.M. / Nair, H.K. / Silman, I. / Sussman, J.L. #1: ![]() Title: Atomic Structure of Acetylcholinesterase from Torpedo Californica: A Prototypic Acetylcholine Binding Enzyme Authors: Sussman, J.L. / Harel, M. / Frolow, F. / Oefner, C. / Goldman, A. / Toker, L. / Silman, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 135.6 KB | Display | ![]() |
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PDB format | ![]() | 111 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 754.5 KB | Display | ![]() |
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Full document | ![]() | 772.5 KB | Display | |
Data in XML | ![]() | 23.4 KB | Display | |
Data in CIF | ![]() | 32.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 104 |
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Components
#1: Protein | Mass: 60736.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Organ: ELECTRIC ORGAN / References: UniProt: P04058, acetylcholinesterase |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-NAF / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.21 Å3/Da / Density % sol: 70.79 % |
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: XENTRONICS / Detector: AREA DETECTOR / Date: May 15, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 25272 / % possible obs: 98 % / Redundancy: 3.08 % / Rmerge(I) obs: 0.118 |
Reflection | *PLUS Highest resolution: 2.8 Å / Rmerge(I) obs: 0.118 |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 22 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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