Zinc 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:

Magnesium

(Mg)

4 atoms

The binding sites of Zinc atom in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2 (pdb code 7b38). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Torpedo Californica Acetylcholinesterase Complexed with Mg+2, PDB code: 7b38:

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Torpedo Californica Acetylcholinesterase Complexed with Mg+2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:46.0 occ:0.63 OE2 A:GLU268 1.9 44.5 1.0 OE1 A:GLU268 2.4 50.6 1.0 CD A:GLU268 2.4 53.0 1.0 NE2 A:HIS264 2.9 49.5 1.0 CD2 A:HIS264 3.4 40.9 1.0 CG A:GLU268 4.0 51.5 1.0 CE1 A:HIS264 4.0 48.5 1.0 MG A:MG619 4.1 59.5 1.0 CG A:HIS264 4.7 36.7 1.0 CB A:GLU268 4.9 43.6 1.0 ND1 A:HIS264 4.9 41.2 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.