Magnesium in PDB 7b38: Torpedo Californica Acetylcholinesterase Complexed with Mg+2

All present enzymatic activity of Torpedo Californica Acetylcholinesterase Complexed with Mg+2:
3.1.1.7;

The structure of Torpedo Californica Acetylcholinesterase Complexed with Mg+2, PDB code: 7b38 was solved by I.Silman, V.L.Shnyrov, Y.Ashani, E.Roth, A.Nicolas, J.L.Sussman, L.Weiner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.83 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	138.217, 138.217, 71.376, 90, 90, 120
R / Rfree (%)	20.2 / 24.1

The structure of Torpedo Californica Acetylcholinesterase Complexed with Mg+2 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2 (pdb code 7b38). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2, PDB code: 7b38:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Torpedo Californica Acetylcholinesterase Complexed with Mg+2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:26.6 occ:1.00 OD2 A:ASP392 2.0 34.8 1.0 OD1 A:ASP326 2.0 26.5 1.0 O A:HOH813 2.1 31.4 1.0 O A:HOH903 2.1 32.4 1.0 O A:HOH873 2.1 26.2 1.0 O A:HOH957 2.2 34.4 1.0 CG A:ASP392 3.1 31.2 1.0 CG A:ASP326 3.2 27.9 1.0 CB A:ASP326 3.8 25.2 1.0 CB A:ASP392 3.9 24.1 1.0 NZ A:LYS325 4.1 40.5 1.0 OD1 A:ASP392 4.1 29.3 1.0 CA A:ASP326 4.1 24.8 1.0 O A:HOH859 4.2 28.9 1.0 OD1 A:ASP393 4.2 25.1 1.0 O A:LYS325 4.2 24.3 1.0 OD2 A:ASP326 4.2 27.9 1.0 O A:HOH939 4.3 38.6 1.0 O A:HOH713 4.4 38.2 1.0 O1 A:EDO613 4.6 42.9 1.0 OD1 A:ASP389 4.6 35.4 1.0 O A:HOH1059 4.7 52.4 1.0 O A:ASP389 4.7 23.7 1.0 O A:HOH882 4.7 33.4 1.0 CG A:ASP393 4.8 26.8 1.0 C A:LYS325 4.8 27.4 1.0 CE A:LYS325 4.9 42.2 1.0 N A:ASP326 4.9 25.2 1.0 CG A:LYS325 4.9 29.2 1.0

Magnesium binding site 2 out of 4 in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Torpedo Californica Acetylcholinesterase Complexed with Mg+2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg618 b:51.4 occ:1.00 ND1 A:HIS471 2.2 50.8 1.0 OE2 A:GLU139 2.6 41.8 1.0 CE1 A:HIS471 2.7 47.6 1.0 CG A:HIS471 2.8 43.8 1.0 OE1 A:GLU139 3.2 42.3 1.0 CD A:GLU139 3.3 42.7 1.0 CB A:HIS471 3.4 39.1 1.0 NE2 A:HIS471 3.5 48.0 1.0 O A:HOH709 3.5 50.7 1.0 CD2 A:HIS471 3.6 45.7 1.0 CA A:HIS471 4.2 41.2 1.0 O A:HOH888 4.5 47.8 1.0 CG A:GLU139 4.8 40.3 1.0 O A:THR138 4.8 47.8 1.0 N A:HIS471 5.0 33.5 1.0 MG A:MG620 5.0 33.0 1.0

Magnesium binding site 3 out of 4 in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Torpedo Californica Acetylcholinesterase Complexed with Mg+2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg619 b:59.5 occ:1.00 CE1 A:HIS264 2.3 48.5 1.0 OE2 A:GLU268 2.4 44.5 1.0 NE2 A:HIS264 2.8 49.5 1.0 CD A:GLU268 3.2 53.0 1.0 CG A:GLU268 3.3 51.5 1.0 ND1 A:HIS264 3.4 41.2 1.0 CD2 A:HIS264 4.1 40.9 1.0 ZN A:ZN602 4.1 46.0 0.6 CG A:HIS264 4.4 36.7 1.0 OE1 A:GLU268 4.4 50.6 1.0 CB A:GLU268 4.8 43.6 1.0

Magnesium binding site 4 out of 4 in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Torpedo Californica Acetylcholinesterase Complexed with Mg+2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg620 b:33.0 occ:1.00 NE2 A:HIS471 1.8 48.0 1.0 CD A:GLU484 2.5 56.0 1.0 CE1 A:HIS471 2.6 47.6 1.0 CD2 A:HIS471 3.0 45.7 1.0 CG A:GLU484 3.6 57.1 1.0 ND1 A:HIS471 3.8 50.8 1.0 CG A:HIS471 4.0 43.8 1.0 OG1 A:THR475 4.1 36.0 1.0 O A:HOH791 4.4 43.2 1.0 CB A:GLU484 4.6 52.4 1.0 CA A:GLU484 4.8 54.0 1.0 MG A:MG618 5.0 51.4 1.0

I.Silman, V.L.Shnyrov, Y.Ashani, E.Roth, A.Nicolas, J.L.Sussman, L.Weiner. Torpedo Californica Acetylcholinesterase Is Stabilized By Binding of A Divalent Metal Ion to A Novel and Versatile 4D Motif To Be Published.