Calcium in PDB 7b8e: Torpedo Californica Acetylcholinesterase Complexed with Ca+2

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

The structure of Torpedo Californica Acetylcholinesterase Complexed with Ca+2, PDB code: 7b8e was solved by I.Silman, V.L.Shnyrov, Y.Ashani, E.Roth, A.Nicolas, J.L.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.23
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	139.074, 139.074, 71.319, 90, 90, 120
R / Rfree (%)	17.9 / 22.6

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

Zinc

(Zn)

1 atom

The binding sites of Calcium atom in the Torpedo Californica Acetylcholinesterase Complexed with Ca+2 (pdb code 7b8e). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Torpedo Californica Acetylcholinesterase Complexed with Ca+2, PDB code: 7b8e:

Calcium binding site 1 out of 1 in the Torpedo Californica Acetylcholinesterase Complexed with Ca+2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Torpedo Californica Acetylcholinesterase Complexed with Ca+2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca606 b:46.5 occ:1.00 OD2 A:ASP392 2.2 47.9 1.0 OD1 A:ASP326 2.2 36.0 1.0 O A:HOH790 2.4 47.7 1.0 O A:HOH747 2.5 33.5 1.0 O A:HOH870 2.6 54.0 1.0 O A:HOH818 2.8 57.7 1.0 CG A:ASP392 3.4 42.5 1.0 CG A:ASP326 3.4 36.4 1.0 CB A:ASP326 4.0 35.3 1.0 CB A:ASP392 4.1 29.1 1.0 O A:HOH729 4.2 43.5 1.0 NZ A:LYS325 4.2 51.6 1.0 OD1 A:ASP393 4.3 36.5 1.0 OD1 A:ASP392 4.3 39.0 1.0 CA A:ASP326 4.4 34.1 1.0 OD2 A:ASP326 4.4 38.8 1.0 O A:LYS325 4.4 34.8 1.0 O A:HOH856 4.5 49.3 1.0 O A:HOH788 4.8 55.5 1.0 O A:ASP389 4.9 29.0 1.0 OD1 A:ASP389 4.9 39.3 1.0 CG A:ASP393 4.9 36.1 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.