Atomistry » Zinc » PDB 1fpp-1g43 » 1fss
Atomistry »
  Zinc »
    PDB 1fpp-1g43 »
      1fss »

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: Wed Dec 16 02:49:41 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy