+Open data
-Basic information
Entry | Database: PDB / ID: 1e3q | ||||||
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Title | TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH BW284C51 | ||||||
Components | ACETYLCHOLINESTERASE | ||||||
Keywords | HYDROLASE / SERINE HYDROLASE / INHIBITOR | ||||||
Function / homology | Function and homology information acetylcholine catabolic process in synaptic cleft / acetylcholinesterase / choline metabolic process / acetylcholinesterase activity / side of membrane / synaptic cleft / synapse / extracellular space / plasma membrane Similarity search - Function | ||||||
Biological species | TORPEDO CALIFORNICA (Pacific electric ray) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.85 Å | ||||||
Authors | Felder, C.E. / Harel, M. / Silman, I. / Sussman, J.L. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2002 Title: Structure of a Complex of the Potent and Specific Inhibitor Bw284C51 with Torpedo Californica Acetylcholinesterase Authors: Felder, C.E. / Harel, M. / Silman, I. / Sussman, J.L. #1: Journal: Structure / Year: 1999 Title: Structure of Acetylcholinesterase Complexed with E2020 (Aricept): Implications for the Design of New Anti-Alzheimer Drugs Authors: Kryger, G. / Silman, I. / Sussman, J.L. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1993 Title: Quaternary Ligand Binding to Aromatic Residues in the Active-Site Gorge of Acetylcholinesterase Authors: Harel, M. / Schalk, I. / Ehret-Sabattier, L. / Bouet, F. / Goeldner, M. / Hirth, C. / Axelsen, P.H. / Silman, I. / Sussman, J.L. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e3q.cif.gz | 124.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e3q.ent.gz | 95.9 KB | Display | PDB format |
PDBx/mmJSON format | 1e3q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1e3q_validation.pdf.gz | 716.2 KB | Display | wwPDB validaton report |
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Full document | 1e3q_full_validation.pdf.gz | 735.4 KB | Display | |
Data in XML | 1e3q_validation.xml.gz | 24.5 KB | Display | |
Data in CIF | 1e3q_validation.cif.gz | 34.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e3/1e3q ftp://data.pdbj.org/pub/pdb/validation_reports/e3/1e3q | HTTPS FTP |
-Related structure data
Related structure data | 2aceS S: Starting model for refinement |
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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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Details | THE ENZYME IS A GPI-ANCHORED DIMER. THE TWO MONOMERS IN THE DIMER ARE RELATED BY CRYSTALLOGRAPHIC TWO-FOLDSYMMETRY. |
-Components
#1: Protein | Mass: 61325.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) TORPEDO CALIFORNICA (Pacific electric ray) Organ: ELECTRIC ORGAN / Tissue: ELECTROPLAQUE / References: UniProt: P04058, acetylcholinesterase | ||
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#2: Chemical | ChemComp-EBW / | ||
#3: Chemical | ChemComp-SO4 / | ||
#4: Sugar | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.23 Å3/Da / Density % sol: 70.9 % | ||||||||||||||||||||
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Crystal grow | pH: 5.8 / Details: pH 5.80 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ / pH: 7 / Method: vapor diffusion, hanging drop / Details: Sussman, J.L., (1991) Science, 253, 872. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418 |
Detector | Type: MULTIWIRE XENTRONICS / Detector: AREA DETECTOR / Date: Dec 15, 1991 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.83→30 Å / Num. obs: 48244 / % possible obs: 77.4 % / Observed criterion σ(I): 0 / Biso Wilson estimate: 39.9 Å2 / Rsym value: 0.104 |
Reflection shell | Resolution: 2.83→3.16 Å / Mean I/σ(I) obs: 2.8 / Rsym value: 0.286 / % possible all: 47 |
Reflection | *PLUS Num. obs: 22837 / Num. measured all: 36141 / Rmerge(I) obs: 0.104 |
Reflection shell | *PLUS % possible obs: 47 % / Rmerge(I) obs: 0.286 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2ACE Resolution: 2.85→18.94 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 8544140.69 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: SEVERAL RESIDUES ARE NOT SEEN IN THE CRYSTAL STRUCTURE, DUE TO DISORDER. THESE INCLUDE ASP 1, ASP 2 AND THE C-TERMINAL RESIDUES AFTER THR 535.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 48.655 Å2 / ksol: 0.329151 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.85→18.94 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.85→3.03 Å / Rfactor Rfree error: 0.037 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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