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Potassium in PDB 2xi4: Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group)

Enzymatic activity of Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group)

All present enzymatic activity of Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group):
3.1.1.7;

Protein crystallography data

The structure of Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group), PDB code: 2xi4 was solved by B.Sanson, J.P.Colletier, Y.Xu, P.T.Lang, H.Jiang, I.Silman, J.L.Sussman, M.Weik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.22 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 91.730, 107.030, 150.730, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 23.4

Other elements in 2xi4:

The structure of Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group) also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group) (pdb code 2xi4). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group), PDB code: 2xi4:

Potassium binding site 1 out of 1 in 2xi4

Go back to Potassium Binding Sites List in 2xi4
Potassium binding site 1 out of 1 in the Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Torpedo Californica Acetylcholinesterase in Complex with Aflatoxin B1 (Orthorhombic Space Group) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1010

b:36.4
occ:1.00
 OE1 A:GLU260 2.3 57.0 0.8
NE2 A:HIS264 2.3 53.4 1.0
CE1 A:HIS264 2.4 55.1 1.0
OE1 A:GLU163 2.7 59.0 0.8
CD A:GLU260 3.1 59.8 0.8
CD A:GLU163 3.5 55.8 0.8
OE2 A:GLU260 3.6 64.9 0.8
CD2 A:HIS264 3.6 53.0 1.0
ND1 A:HIS264 3.6 56.2 1.0
CG A:GLU163 4.1 52.7 1.0
CG A:GLU260 4.2 56.9 1.0
OE2 A:GLU163 4.2 56.1 0.8
CG A:HIS264 4.2 51.0 1.0
NH1 A:ARG267 4.4 44.3 1.0
O A:HOH2125 4.5 24.3 1.0
O A:GLU260 4.9 49.6 1.0
CB A:GLU260 4.9 53.0 1.0

Reference:

B.Sanson, J.P.Colletier, Y.Xu, P.T.Lang, H.Jiang, I.Silman, J.L.Sussman, M.Weik. Backdoor Opening Mechanism in Acetylcholinesterase Based on X-Ray Crystallography and Molecular Dynamics Simulations. Protein Sci. V. 20 1114 2011.
ISSN: ISSN 0961-8368
PubMed: 21594947
DOI: 10.1002/PRO.661
Page generated: Mon Aug 12 07:38:49 2024

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