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Fluorine in PDB 2h9y: Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone

Enzymatic activity of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone

All present enzymatic activity of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone:
3.1.1.7;

Protein crystallography data

The structure of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone, PDB code: 2h9y was solved by Y.Bourne, Z.Radic, G.Sulzenbacher, E.Kim, P.Taylor, P.Marchot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.013, 111.394, 226.934, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 21.4

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone (pdb code 2h9y). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone, PDB code: 2h9y:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 2h9y

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Fluorine binding site 1 out of 6 in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F951

b:55.0
occ:1.00
 F1' A:NAF951 0.0 55.0 1.0
C2' A:NAF951 1.3 54.2 1.0
F3' A:NAF951 2.1 53.8 1.0
F2' A:NAF951 2.2 55.9 1.0
C1' A:NAF951 2.3 54.3 1.0
O1' A:NAF951 2.9 51.5 1.0
C4 A:NAF951 2.9 55.6 1.0
CZ A:PHE297 3.0 46.4 1.0
C3 A:NAF951 3.0 55.7 1.0
CA A:GLY122 3.0 46.8 1.0
CE2 A:PHE297 3.1 46.3 1.0
N A:GLY122 3.3 46.0 1.0
OG A:SER203 3.8 49.4 1.0
CE1 A:PHE297 3.9 47.9 1.0
CD2 A:PHE297 4.0 46.4 1.0
CE1 A:PHE295 4.2 50.9 1.0
C5 A:NAF951 4.2 56.8 1.0
C2 A:NAF951 4.3 54.6 1.0
C A:GLY121 4.4 46.1 1.0
C A:GLY122 4.4 47.4 1.0
CZ3 A:TRP236 4.5 50.2 1.0
CE3 A:TRP236 4.7 51.6 1.0
CD1 A:PHE297 4.7 47.9 1.0
CD1 A:PHE295 4.7 51.6 1.0
CE2 A:PHE338 4.7 50.8 1.0
N A:ALA204 4.7 48.2 1.0
CG A:PHE297 4.7 48.7 1.0
CH2 A:TRP236 4.8 49.7 1.0
CZ A:PHE295 4.8 50.8 1.0
CB A:ALA204 4.8 48.1 1.0
CZ A:PHE338 4.9 49.3 1.0
CB A:SER203 4.9 48.4 1.0
O A:GLY122 5.0 47.9 1.0

Fluorine binding site 2 out of 6 in 2h9y

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Fluorine binding site 2 out of 6 in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F951

b:55.9
occ:1.00
 F2' A:NAF951 0.0 55.9 1.0
C2' A:NAF951 1.3 54.2 1.0
F3' A:NAF951 2.1 53.8 1.0
F1' A:NAF951 2.2 55.0 1.0
C1' A:NAF951 2.3 54.3 1.0
OG A:SER203 2.8 49.4 1.0
C3 A:NAF951 2.9 55.7 1.0
C4 A:NAF951 3.2 55.6 1.0
CE1 A:PHE295 3.2 50.9 1.0
CZ A:PHE295 3.3 50.8 1.0
CZ A:PHE338 3.3 49.3 1.0
O1' A:NAF951 3.5 51.5 1.0
NE2 A:HIS447 3.6 51.7 1.0
CE2 A:PHE338 3.7 50.8 1.0
C2 A:NAF951 4.1 54.6 1.0
CD1 A:PHE295 4.1 51.6 1.0
CE2 A:PHE295 4.2 49.9 1.0
CZ A:PHE297 4.2 46.4 1.0
CB A:SER203 4.2 48.4 1.0
CE1 A:HIS447 4.2 51.5 1.0
CD2 A:HIS447 4.3 50.0 1.0
CE1 A:PHE338 4.4 50.0 1.0
C5 A:NAF951 4.5 56.8 1.0
CE2 A:PHE297 4.5 46.3 1.0
CZ2 A:TRP236 4.8 49.9 1.0
CD2 A:PHE295 4.9 51.4 1.0
CG A:PHE295 4.9 51.3 1.0
CA A:SER203 4.9 48.3 1.0
CH2 A:TRP236 4.9 49.7 1.0
CD2 A:PHE338 5.0 50.2 1.0

Fluorine binding site 3 out of 6 in 2h9y

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Fluorine binding site 3 out of 6 in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F951

b:53.8
occ:1.00
 F3' A:NAF951 0.0 53.8 1.0
C2' A:NAF951 1.3 54.2 1.0
F1' A:NAF951 2.1 55.0 1.0
F2' A:NAF951 2.1 55.9 1.0
C1' A:NAF951 2.4 54.3 1.0
OG A:SER203 2.6 49.4 1.0
O1' A:NAF951 2.7 51.5 1.0
CH2 A:TRP236 3.1 49.7 1.0
N A:ALA204 3.3 48.2 1.0
CZ3 A:TRP236 3.4 50.2 1.0
CZ2 A:TRP236 3.5 49.9 1.0
CB A:SER203 3.7 48.4 1.0
C3 A:NAF951 3.7 55.7 1.0
C A:SER203 3.7 48.2 1.0
CA A:SER203 3.9 48.3 1.0
CE1 A:PHE295 3.9 50.9 1.0
CE3 A:TRP236 4.0 51.6 1.0
CE2 A:TRP236 4.0 50.9 1.0
CA A:ALA204 4.1 48.6 1.0
CD2 A:TRP236 4.3 51.5 1.0
CE2 A:PHE297 4.3 46.3 1.0
C4 A:NAF951 4.3 55.6 1.0
CB A:ALA204 4.3 48.1 1.0
CZ A:PHE295 4.3 50.8 1.0
CA A:GLY122 4.4 46.8 1.0
N A:GLY122 4.4 46.0 1.0
O A:SER203 4.5 49.4 1.0
CZ A:PHE297 4.6 46.4 1.0
NE2 A:HIS447 4.7 51.7 1.0
C2 A:NAF951 4.8 54.6 1.0
CD1 A:PHE295 4.9 51.6 1.0
NE1 A:TRP236 5.0 51.6 1.0

Fluorine binding site 4 out of 6 in 2h9y

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Fluorine binding site 4 out of 6 in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F952

b:64.0
occ:1.00
 F1' B:NAF952 0.0 64.0 1.0
C2' B:NAF952 1.3 61.3 1.0
F3' B:NAF952 2.1 61.2 1.0
F2' B:NAF952 2.2 60.9 1.0
C1' B:NAF952 2.3 60.2 1.0
O1' B:NAF952 2.7 58.6 1.0
CA B:GLY122 2.9 53.8 1.0
C3 B:NAF952 3.0 60.2 1.0
C4 B:NAF952 3.0 60.2 1.0
CE2 B:PHE297 3.0 55.4 1.0
CZ B:PHE297 3.0 55.7 1.0
N B:GLY122 3.1 53.4 1.0
OG B:SER203 3.7 52.8 1.0
CD2 B:PHE297 4.0 55.7 1.0
CE1 B:PHE297 4.0 57.8 1.0
C B:GLY121 4.2 53.8 1.0
C2 B:NAF952 4.3 59.9 1.0
C B:GLY122 4.3 53.8 1.0
C5 B:NAF952 4.4 61.0 1.0
CZ3 B:TRP236 4.4 53.7 1.0
CE1 B:PHE295 4.4 54.4 1.0
N B:ALA204 4.5 52.2 1.0
CB B:ALA204 4.5 51.6 1.0
CE3 B:TRP236 4.6 55.4 1.0
CD1 B:PHE297 4.7 58.3 1.0
CG B:PHE297 4.7 57.4 1.0
CH2 B:TRP236 4.8 53.1 1.0
CB B:SER203 4.9 53.1 1.0
O B:GLY122 4.9 54.3 1.0
N B:GLY121 4.9 52.6 1.0
CD1 B:PHE295 4.9 56.7 1.0
CE2 B:PHE338 4.9 59.2 1.0
CA B:GLY121 5.0 53.2 1.0
CZ B:PHE295 5.0 54.8 1.0
CA B:ALA204 5.0 52.2 1.0

Fluorine binding site 5 out of 6 in 2h9y

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Fluorine binding site 5 out of 6 in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F952

b:60.9
occ:1.00
 F2' B:NAF952 0.0 60.9 1.0
C2' B:NAF952 1.3 61.3 1.0
F3' B:NAF952 2.1 61.2 1.0
F1' B:NAF952 2.2 64.0 1.0
C1' B:NAF952 2.3 60.2 1.0
OG B:SER203 2.9 52.8 1.0
C3 B:NAF952 3.0 60.2 1.0
C4 B:NAF952 3.2 60.2 1.0
CE1 B:PHE295 3.2 54.4 1.0
CZ B:PHE295 3.2 54.8 1.0
CZ B:PHE338 3.3 58.3 1.0
O1' B:NAF952 3.6 58.6 1.0
CE2 B:PHE338 3.6 59.2 1.0
NE2 B:HIS447 3.8 59.5 1.0
CZ B:PHE297 3.9 55.7 1.0
CD1 B:PHE295 4.1 56.7 1.0
CE2 B:PHE295 4.1 56.2 1.0
C2 B:NAF952 4.2 59.9 1.0
CE1 B:HIS447 4.2 59.1 1.0
CE2 B:PHE297 4.2 55.4 1.0
CB B:SER203 4.3 53.1 1.0
C5 B:NAF952 4.4 61.0 1.0
CE1 B:PHE338 4.5 58.3 1.0
CD2 B:HIS447 4.6 60.3 1.0
CD2 B:PHE295 4.8 58.3 1.0
CG B:PHE295 4.8 58.6 1.0
CD2 B:PHE338 4.9 59.3 1.0
CH2 B:TRP236 5.0 53.1 1.0
CZ2 B:TRP236 5.0 53.2 1.0

Fluorine binding site 6 out of 6 in 2h9y

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Fluorine binding site 6 out of 6 in the Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Mouse Acetylcholinesterase Complexed with M-(N,N, N-Trimethylammonio)Trifluoroacetophenone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F952

b:61.2
occ:1.00
 F3' B:NAF952 0.0 61.2 1.0
C2' B:NAF952 1.3 61.3 1.0
F2' B:NAF952 2.1 60.9 1.0
F1' B:NAF952 2.1 64.0 1.0
C1' B:NAF952 2.4 60.2 1.0
OG B:SER203 2.6 52.8 1.0
O1' B:NAF952 2.8 58.6 1.0
CH2 B:TRP236 3.2 53.1 1.0
N B:ALA204 3.3 52.2 1.0
CZ3 B:TRP236 3.4 53.7 1.0
CZ2 B:TRP236 3.6 53.2 1.0
CB B:SER203 3.6 53.1 1.0
C B:SER203 3.7 52.2 1.0
C3 B:NAF952 3.7 60.2 1.0
CA B:SER203 3.9 52.4 1.0
CE1 B:PHE295 3.9 54.4 1.0
CE3 B:TRP236 4.0 55.4 1.0
CA B:ALA204 4.1 52.2 1.0
CE2 B:TRP236 4.2 55.3 1.0
CE2 B:PHE297 4.3 55.4 1.0
CZ B:PHE295 4.3 54.8 1.0
CB B:ALA204 4.3 51.6 1.0
C4 B:NAF952 4.3 60.2 1.0
CD2 B:TRP236 4.4 54.2 1.0
O B:SER203 4.5 53.0 1.0
N B:GLY122 4.5 53.4 1.0
CA B:GLY122 4.5 53.8 1.0
CZ B:PHE297 4.6 55.7 1.0
NE2 B:HIS447 4.6 59.5 1.0
C2 B:NAF952 4.7 59.9 1.0
CE1 B:HIS447 4.9 59.1 1.0
CD1 B:PHE295 5.0 56.7 1.0

Reference:

Y.Bourne, Z.Radic, G.Sulzenbacher, E.Kim, P.Taylor, P.Marchot. Substrate and Product Trafficking Through the Active Center Gorge of Acetylcholinesterase Analyzed By Crystallography and Equilibrium Binding J.Biol.Chem. V. 281 29256 2006.
ISSN: ISSN 0021-9258
PubMed: 16837465
DOI: 10.1074/JBC.M603018200
Page generated: Wed Jul 31 14:41:45 2024

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