Magnesium in PDB 2j3q: Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T

All present enzymatic activity of Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T:
3.1.1.7;

The structure of Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T, PDB code: 2j3q was solved by M.Harel, B.Cusack, J.L.Johnson, I.Silman, J.L.Sussman, T.L.Rosenberry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.81 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	139.440, 139.440, 71.420, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 25.7

The binding sites of Magnesium atom in the Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T (pdb code 2j3q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T, PDB code: 2j3q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1542 b:15.7 occ:1.00 OE1 A:GLU268 2.2 40.5 1.0 NE2 A:HIS264 2.6 39.9 1.0 CD2 A:HIS264 2.9 42.1 1.0 CD A:GLU268 3.0 41.8 1.0 OE2 A:GLU268 3.3 37.4 1.0 CE1 A:HIS264 3.9 43.1 1.0 CG A:HIS264 4.2 41.3 1.0 CG A:GLU268 4.3 42.1 1.0 ND1 A:HIS264 4.7 43.3 1.0

Magnesium binding site 2 out of 2 in the Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Torpedo Acetylcholinesterase Complexed with Fluorophore Thioflavin T within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1543 b:18.9 occ:1.00 OD2 A:ASP392 2.3 20.3 1.0 O A:HOH2065 2.3 34.4 1.0 OD1 A:ASP326 2.4 22.4 1.0 CG A:ASP392 3.4 23.4 1.0 CG A:ASP326 3.6 23.5 1.0 CB A:ASP392 3.9 20.4 1.0 NZ A:LYS325 4.1 27.2 1.0 OD1 A:ASP389 4.1 26.5 1.0 OD1 A:ASP393 4.2 26.1 1.0 CB A:ASP326 4.3 21.1 1.0 O A:ASP389 4.5 26.7 1.0 CG A:ASP389 4.5 28.1 1.0 CB A:ASP389 4.5 26.7 1.0 OD1 A:ASP392 4.5 22.4 1.0 O A:LYS325 4.6 22.5 1.0 OD2 A:ASP326 4.6 24.2 1.0 CA A:ASP389 4.7 26.7 1.0 CG A:ASP393 4.7 23.6 1.0 OD2 A:ASP393 4.8 23.6 1.0 CA A:ASP326 4.8 20.1 1.0 CE A:LYS325 5.0 25.3 1.0

M.Harel, L.K.Sonoda, I.Silman, J.L.Sussman, T.L.Rosenberry. Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo Californica Acetylcholinesterase Reveals How Thioflavin T Acts As A Sensitive Fluorescent Reporter of Ligand Binding to the Acylation Site. J. Am. Chem. Soc. V. 130 7856 2008.
ISSN: ESSN 1520-5126
PubMed: 18512913
DOI: 10.1021/JA7109822