+Open data
-Basic information
Entry | Database: PDB / ID: 1fss | ||||||
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Title | ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH FASCICULIN-II | ||||||
Components |
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Keywords | COMPLEX (SERINE ESTERASE/TOXIN) / COMPLEX (SERINE ESTERASE-TOXIN) / COMPLEX (SERINE ESTERASE-TOXIN) complex | ||||||
Function / homology | Function and homology information acetylcholine catabolic process in synaptic cleft / acetylcholinesterase / acetylcholinesterase activity / choline metabolic process / side of membrane / synaptic cleft / toxin activity / synapse / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Torpedo californica (Pacific electric ray) Dendroaspis angusticeps (eastern green mamba) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3 Å | ||||||
Authors | Harel, M. / Kleywegt, G.J. / Silman, I. / Sussman, J.L. | ||||||
Citation | Journal: Structure / Year: 1995 Title: Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target. Authors: Harel, M. / Kleywegt, G.J. / Ravelli, R.B. / Silman, I. / Sussman, J.L. #1: Journal: J.Biol.Chem. / Year: 1992 Title: 1.9-Angstroms Resolution Structure of Fasciculin 1, an Anti-Acetylcholine Esterase Toxin from Green Mamba Snake Venom Authors: Le Du, M.H. / Marchot, P. / Bougis, P.E. / Fontecilla-Camps, J.C. #2: Journal: Science / Year: 1991 Title: Atomic Structure of Acetylcholine Esterase 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fss.cif.gz | 112.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fss.ent.gz | 91.8 KB | Display | PDB format |
PDBx/mmJSON format | 1fss.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fss_validation.pdf.gz | 462.9 KB | Display | wwPDB validaton report |
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Full document | 1fss_full_validation.pdf.gz | 479.3 KB | Display | |
Data in XML | 1fss_validation.xml.gz | 24.2 KB | Display | |
Data in CIF | 1fss_validation.cif.gz | 32.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fs/1fss ftp://data.pdbj.org/pub/pdb/validation_reports/fs/1fss | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-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 A 104 / 2: CIS PROLINE - PRO B 31 / 3: CIS PROLINE - PRO B 56 | ||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 60736.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Torpedo californica (Pacific electric ray) Organ: ELECTRIC ORGAN / Variant: G2 FORM / Tissue: ELECTROPLAQUE / References: UniProt: P04058, acetylcholinesterase | ||
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#2: Protein | Mass: 6768.769 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) Dendroaspis angusticeps (eastern green mamba) Organ: ELECTRIC ORGAN / Tissue: VENOM / References: UniProt: P01403, UniProt: P0C1Z0*PLUS | ||
#3: Sugar | ChemComp-NAG / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 50.99 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 5.2 / Method: vapor diffusionDetails: drop solution was mixed with an equal volume of reservoir solution | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 1.15 |
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Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Nov 15, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.15 Å / Relative weight: 1 |
Reflection | Num. obs: 14206 / % possible obs: 97.7 % / Redundancy: 3.43 % / Rmerge(I) obs: 0.105 |
Reflection | *PLUS Highest resolution: 3 Å / Num. measured all: 48744 / Rmerge(I) obs: 0.105 |
Reflection shell | *PLUS Highest resolution: 3 Å / Lowest resolution: 3.11 Å / % possible obs: 93.7 % / Rmerge(I) obs: 0.303 / Mean I/σ(I) obs: 3.5 |
-Processing
Software |
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Refinement | Resolution: 3→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 19.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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