Iodine in PDB 1qon: Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine

Enzymatic activity of Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine

All present enzymatic activity of Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine:
3.1.1.7;

Protein crystallography data

The structure of Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine, PDB code: 1qon was solved by M.Harel, I.Silman, J.L.Sussman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.72
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 94.930, 94.930, 160.020, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 26.5

Iodine Binding Sites:

The binding sites of Iodine atom in the Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine (pdb code 1qon). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total only one binding site of Iodine was determined in the Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine, PDB code: 1qon:

Iodine binding site 1 out of 1 in 1qon

Go back to Iodine Binding Sites List in 1qon
Iodine binding site 1 out of 1 in the Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Ache From Drosophila Melanogaster Complex with Tacrine Derivative 9- (3-Iodobenzylamino)-1,2,3,4-Tetrahydroacridine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I997

b:86.8
occ:0.60
 I1 A:I40997 0.0 86.8 0.6
C17 A:I40997 2.0 87.7 1.0
O A:HOH2138 2.5 23.7 1.0
C18 A:I40997 2.9 87.6 1.0
C16 A:I40997 3.0 87.3 1.0
CZ A:PHE330 3.2 55.0 1.0
CE1 A:PHE330 3.3 53.8 1.0
OH A:TYR71 4.0 74.8 1.0
CE1 A:PHE371 4.0 40.0 1.0
C19 A:I40997 4.2 86.3 1.0
C15 A:I40997 4.3 86.1 1.0
CE2 A:PHE330 4.3 56.3 1.0
O4 A:SO4593 4.3 62.7 1.0
O A:GLY150 4.3 28.8 1.0
CD1 A:PHE330 4.4 53.8 1.0
C A:GLY150 4.4 30.1 1.0
N A:GLY151 4.6 30.2 1.0
CA A:GLY151 4.6 32.5 1.0
O1 A:SO4593 4.7 55.1 1.0
CZ A:TYR71 4.7 73.3 1.0
C20 A:I40997 4.8 85.6 1.0
CD1 A:PHE371 4.9 42.1 1.0
CZ A:PHE371 4.9 39.8 1.0

Reference:

M.Harel, G.Kryger, T.L.Rosenberry, W.D.Mallender, T.Lewis, R.J.Fletcher, J.M.Guss, I.Silman, J.L.Sussman. Three-Dimensional Structures of Drosophila Melanogaster Acetylcholinesterase and of Its Complexes with Two Potent Inhibitors. Protein Sci. V. 9 1063 2000.
ISSN: ISSN 0961-8368
PubMed: 10892800
DOI: 10.1110/PS.9.6.1063
Page generated: Sun Dec 13 19:21:07 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