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
Acetylcholinesterase, fish/snake / 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, catalytic domain / Alpha/Beta hydrolase fold ...Acetylcholinesterase, fish/snake / 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, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology
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 / Variant: G2 FORM / Tissue: ELECTROPLAQUE / References: UniProt: P04058, acetylcholinesterase
Type: RIGAKU RAXIS4++ / Detector: IMAGE PLATE / Date: Oct 31, 2000 / Details: OSMIC BLUE
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.5418 Å / Relative weight: 1
Reflection
Resolution: 2.15→30 Å / Num. obs: 80692 / % possible obs: 92 % / Redundancy: 2.9 % / Biso Wilson estimate: 24.1 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 10.8
Reflection shell
Resolution: 2.15→2.23 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.51 / % possible all: 75.6
-
Processing
Software
Name
Version
Classification
CNS
1.1
refinement
DENZO
datareduction
SCALEPACK
datascaling
Refinement
Method to determine structure: OTHER / Resolution: 2.15→29.27 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2192213.75 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF Details: THE BIOLOGICALLY ACTIVE FORM OF THIS MOLECULE IS A DIMER, FORMED BY ROTATING THE ASYMMETRIC UNIT ABOUT THE CRYSTALLOGRAPHIC TWO-FOLD AXIS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.249
2517
5 %
RANDOM
Rwork
0.211
-
-
-
obs
0.211
50424
92 %
-
Solvent computation
Solvent model: CNS BULK SOLVENT MODEL USED / Bsol: 40.9311 Å2 / ksol: 0.338604 e/Å3
Displacement parameters
Biso mean: 44.05 Å2
Baniso -1
Baniso -2
Baniso -3
1-
8.34 Å2
6.53 Å2
0 Å2
2-
-
8.34 Å2
0 Å2
3-
-
-
-16.69 Å2
Refine analyze
Free
Obs
Luzzati coordinate error
0.34 Å
0.29 Å
Luzzati d res low
-
5 Å
Luzzati sigma a
0.51 Å
0.53 Å
Refinement step
Cycle: LAST / Resolution: 2.15→29.27 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
4142
0
65
206
4413
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
X-RAY DIFFRACTION
c_bond_d
0.018
X-RAY DIFFRACTION
c_bond_d_na
X-RAY DIFFRACTION
c_bond_d_prot
X-RAY DIFFRACTION
c_angle_d
X-RAY DIFFRACTION
c_angle_d_na
X-RAY DIFFRACTION
c_angle_d_prot
X-RAY DIFFRACTION
c_angle_deg
1.9
X-RAY DIFFRACTION
c_angle_deg_na
X-RAY DIFFRACTION
c_angle_deg_prot
X-RAY DIFFRACTION
c_dihedral_angle_d
X-RAY DIFFRACTION
c_dihedral_angle_d_na
X-RAY DIFFRACTION
c_dihedral_angle_d_prot
X-RAY DIFFRACTION
c_improper_angle_d
X-RAY DIFFRACTION
c_improper_angle_d_na
X-RAY DIFFRACTION
c_improper_angle_d_prot
X-RAY DIFFRACTION
c_mcbond_it
1.12
1.5
X-RAY DIFFRACTION
c_mcangle_it
1.81
2
X-RAY DIFFRACTION
c_scbond_it
6.55
2
X-RAY DIFFRACTION
c_scangle_it
7.1
2.5
LS refinement shell
Resolution: 2.15→2.16 Å / Total num. of bins used: 50
Rfactor
Num. reflection
% reflection
Rfree
0.38
35
5 %
Rwork
0.42
716
-
+
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