SASBDB entries for UniProt ID: P22303

SASDL82 – Human acetylcholinesterase, apo

UniProt ID: P22303-1 (32-578) acetylcholinesterase

UniProt ID: P22303-1 (32-578) acetylcholinesterase
acetylcholinesteraseacetylcholinesterase experimental SAS data
OTHER model
Sample: Acetylcholinesterase dimer, 120 kDa Homo sapiens protein
Acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. J Biol Chem :101007 (2021)
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 162 nm3

SASDL92 – Human acetylcholinesterase, covalently bound to paraoxon

UniProt ID: P22303-1 (32-578) acetylcholinesterase

UniProt ID: P22303-1 (32-578) acetylcholinesterase
acetylcholinesteraseacetylcholinesterase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Acetylcholinesterase dimer, 120 kDa Homo sapiens protein
Acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. J Biol Chem :101007 (2021)
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 142 nm3