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

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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

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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

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