Zinc in PDB 8aen: Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium

Enzymatic activity of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium

All present enzymatic activity of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium:
3.1.1.7;

Protein crystallography data

The structure of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium, PDB code: 8aen was solved by F.Nachon, J.Dias, X.Brazzolotto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.30 / 3.01
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 210.85, 210.85, 114.76, 90, 90, 120
R / Rfree (%) 16.2 / 19.6

Other elements in 8aen:

The structure of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium also contains other interesting chemical elements:

Chlorine (Cl) 36 atoms
Magnesium (Mg) 12 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium (pdb code 8aen). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium, PDB code: 8aen:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 8aen

Go back to Zinc Binding Sites List in 8aen
Zinc binding site 1 out of 4 in the Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:69.7
occ:1.00
 OG A:SER203 2.1 72.1 1.0
O07 A:LWL601 2.2 71.7 1.0
N09 A:LWL601 2.2 76.3 1.0
N16 A:LWL601 2.2 73.5 1.0
NE2 A:HIS447 2.3 71.9 1.0
CB A:SER203 2.8 65.9 1.0
C06 A:LWL601 2.8 74.7 1.0
C10 A:LWL601 2.9 72.8 1.0
C11 A:LWL601 2.9 74.9 1.0
N08 A:LWL601 3.1 76.2 1.0
CE1 A:HIS447 3.1 71.8 1.0
CD2 A:HIS447 3.3 72.8 1.0
C15 A:LWL601 3.3 74.2 1.0
CA A:SER203 3.9 65.7 1.0
N A:GLY122 4.0 63.9 1.0
CZ A:PHE338 4.1 80.0 1.0
ND1 A:HIS447 4.2 72.4 1.0
C12 A:LWL601 4.3 81.2 1.0
C05 A:LWL601 4.3 76.1 1.0
CG A:HIS447 4.3 74.0 1.0
CE1 A:PHE338 4.4 83.8 1.0
N A:GLY121 4.4 63.8 1.0
C04 A:LWL601 4.5 83.0 1.0
N A:ALA204 4.5 66.4 1.0
C14 A:LWL601 4.5 78.0 1.0
CA A:GLY121 4.6 63.8 1.0
CA A:GLY122 4.7 65.5 1.0
C A:SER203 4.7 64.1 1.0
C A:GLY121 4.7 65.9 1.0
C13 A:LWL601 4.9 87.2 1.0
OE1 A:GLU202 4.9 70.6 1.0
N02 A:LWL601 5.0 83.0 1.0

Zinc binding site 2 out of 4 in 8aen

Go back to Zinc Binding Sites List in 8aen
Zinc binding site 2 out of 4 in the Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn631

b:116.6
occ:1.00
 ND1 A:HIS381 2.3 86.7 1.0
NE2 B:HIS381 2.3 99.9 1.0
CE1 B:HIS381 2.6 99.6 1.0
CE1 A:HIS381 3.1 93.1 1.0
CG A:HIS381 3.4 80.8 1.0
CD2 B:HIS381 3.6 91.0 1.0
CA A:HIS381 3.8 84.9 1.0
CB A:HIS381 3.8 80.6 1.0
CL B:CL622 3.9 89.2 1.0
ND1 B:HIS381 3.9 93.0 1.0
NE2 A:HIS381 4.3 100.9 1.0
N A:HIS381 4.3 83.8 1.0
CD2 A:HIS381 4.4 86.8 1.0
CG B:HIS381 4.4 89.0 1.0
CD1 B:PHE531 4.5 73.8 1.0
C A:LEU380 4.7 87.3 1.0
O A:LEU380 4.7 87.7 1.0
O A:ALA377 5.0 88.6 1.0
CB B:PHE531 5.0 75.0 1.0

Zinc binding site 3 out of 4 in 8aen

Go back to Zinc Binding Sites List in 8aen
Zinc binding site 3 out of 4 in the Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn632

b:117.9
occ:1.00
 NE2 A:HIS287 2.4 91.3 1.0
CE1 A:HIS287 2.5 95.1 1.0
O A:HOH777 2.9 90.4 1.0
CL A:CL619 2.9 111.8 1.0
CL A:CL622 3.4 108.0 1.0
O A:HOH771 3.6 95.2 1.0
CD2 A:HIS287 3.6 84.7 1.0
ND1 A:HIS287 3.7 93.0 1.0
CG A:HIS287 4.3 81.7 1.0
O A:ASN283 4.8 82.4 1.0
CB A:TRP286 4.8 77.7 1.0

Zinc binding site 4 out of 4 in 8aen

Go back to Zinc Binding Sites List in 8aen
Zinc binding site 4 out of 4 in the Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Acetylcholinesterase in Complex with Zinc and N,N,N-Trimethyl-2- Oxo-2-(2-(Pyridin-2-Ylmethylene)Hydrazineyl)Ethan-1-Aminium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:83.2
occ:1.00
 O07 B:LWL601 1.8 94.7 1.0
OG B:SER203 2.2 74.6 1.0
C10 B:LWL601 2.2 89.8 1.0
NE2 B:HIS447 2.3 75.0 1.0
N16 B:LWL601 2.5 90.8 1.0
C06 B:LWL601 2.6 95.2 1.0
N09 B:LWL601 2.6 92.1 1.0
C11 B:LWL601 2.7 93.3 1.0
CB B:SER203 2.7 69.5 1.0
N08 B:LWL601 3.1 93.9 1.0
CD2 B:HIS447 3.2 76.0 1.0
CE1 B:HIS447 3.2 72.9 1.0
C15 B:LWL601 3.7 90.4 1.0
CA B:SER203 3.8 66.1 1.0
C05 B:LWL601 3.9 91.3 1.0
C12 B:LWL601 4.1 97.1 1.0
N B:GLY122 4.1 72.1 1.0
ND1 B:HIS447 4.3 76.0 1.0
CG B:HIS447 4.3 73.5 1.0
CE1 B:PHE338 4.4 86.5 1.0
N B:ALA204 4.4 62.8 1.0
N B:GLY121 4.4 71.2 1.0
CZ B:PHE338 4.5 83.4 1.0
C B:SER203 4.5 64.2 1.0
CA B:GLY122 4.7 68.4 1.0
C01 B:LWL601 4.7 96.3 1.0
C14 B:LWL601 4.8 95.1 1.0
N02 B:LWL601 4.9 98.1 1.0
CA B:GLY121 4.9 73.0 1.0
C B:GLY121 4.9 72.2 1.0
C13 B:LWL601 5.0 100.2 1.0
N B:SER203 5.0 68.4 1.0
OE1 B:GLU202 5.0 72.8 1.0

Reference:

F.Nachon, X.Brazzolotto, J.Dias, C.Courageux, W.Drozdz, X.Y.Cao, A.R.Stefankiewicz, J.M.Lehn. Grid-Type Quaternary Metallosupramolecular Compounds Inhibit Human Cholinesterases Through Dynamic Multivalent Interactions. Chembiochem V. 23 00456 2022.
ISSN: ESSN 1439-7633
PubMed: 36193860
DOI: 10.1002/CBIC.202200456
Page generated: Wed Oct 30 17:43:31 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy