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Zinc in PDB 1fss: Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II

Enzymatic activity of Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II

All present enzymatic activity of Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II:
3.1.1.7;

Protein crystallography data

The structure of Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II, PDB code: 1fss was solved by M.Harel, G.J.Kleywegt, I.Silman, J.L.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 3.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 87.390, 115.000, 67.470, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 31

Zinc Binding Sites:

The binding sites of Zinc atom in the Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II (pdb code 1fss). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II, PDB code: 1fss:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1fss

Go back to Zinc Binding Sites List in 1fss
Zinc binding site 1 out of 2 in the Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:19.8
occ:1.00
OE2 A:GLU350 2.5 26.1 1.0
OE1 A:GLU350 2.6 26.1 1.0
CD A:GLU350 2.9 26.1 1.0
CG A:GLU350 4.4 26.1 1.0

Zinc binding site 2 out of 2 in 1fss

Go back to Zinc Binding Sites List in 1fss
Zinc binding site 2 out of 2 in the Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Acetylcholinesterase (E.C. 3.1.1.7) Complexed with Fasciculin-II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn902

b:19.2
occ:1.00
OE1 A:GLU49 2.5 40.0 1.0
OE2 A:GLU49 2.6 40.0 1.0
CD A:GLU49 2.9 40.0 1.0
CG A:GLU49 4.3 40.0 1.0
CD A:PRO50 4.7 12.7 1.0
CB A:GLU49 4.9 40.0 1.0

Reference:

M.Harel, G.J.Kleywegt, R.B.Ravelli, I.Silman, J.L.Sussman. Crystal Structure of An Acetylcholinesterase-Fasciculin Complex: Interaction of A Three-Fingered Toxin From Snake Venom with Its Target. Structure V. 3 1355 1995.
ISSN: ISSN 0969-2126
PubMed: 8747462
DOI: 10.1016/S0969-2126(01)00273-8
Page generated: Sun Oct 13 01:07:13 2024

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