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

Enzymatic activity of Torpedo Californica Acetylcholinesterase Complexed with Ca+2

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

Protein crystallography data

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

Other elements in 7b8e:

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

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Torpedo Californica Acetylcholinesterase Complexed with Ca+2 (pdb code 7b8e). 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 Ca+2, PDB code: 7b8e:

Zinc binding site 1 out of 1 in 7b8e

Go back to Zinc Binding Sites List in 7b8e
Zinc 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 Zinc with other atoms in the Zn binding site number 1 of Torpedo Californica Acetylcholinesterase Complexed with Ca+2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn607

b:65.5
occ:1.00
NE2 A:HIS264 2.0 54.5 1.0
OE1 A:GLU268 2.2 64.8 1.0
CD A:GLU268 2.8 57.8 1.0
CE1 A:HIS264 2.9 53.0 1.0
CD2 A:HIS264 3.1 39.3 1.0
OE2 A:GLU268 3.4 63.2 1.0
CG A:GLU268 3.6 54.7 1.0
O A:HOH843 3.6 53.7 1.0
ND1 A:HIS264 4.0 51.0 1.0
CG A:HIS264 4.2 46.3 1.0
O A:HOH731 4.4 47.3 1.0
CB A:GLU268 5.0 49.3 1.0

Reference:

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.
Page generated: Tue Oct 29 17:32:03 2024

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