Chlorine in PDB 7ly8: The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring

Enzymatic activity of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring

All present enzymatic activity of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring:
4.2.1.20;

Protein crystallography data

The structure of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring, PDB code: 7ly8 was solved by E.Hilario, M.F.Dunn, L.J.Mueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.85 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.645, 58.8, 67.205, 90, 95.13, 90
R / Rfree (%) 17.3 / 19.4

Other elements in 7ly8:

The structure of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring also contains other interesting chemical elements:

Fluorine (F) 9 atoms
Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring (pdb code 7ly8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring, PDB code: 7ly8:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in 7ly8

Go back to Chlorine Binding Sites List in 7ly8
Chlorine binding site 1 out of 5 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:64.3
occ:1.00
 O A:HOH601 4.0 49.9 1.0
CB A:SER168 4.2 24.7 1.0
OH A:TYR169 4.2 37.3 1.0
OG A:SER168 4.2 28.1 1.0
CZ A:TYR169 4.5 33.8 1.0
O A:ARG164 4.6 22.5 1.0
CA A:GLN165 4.9 22.0 1.0
CG A:GLN165 4.9 27.3 1.0
CE2 A:TYR169 4.9 31.6 1.0
CE1 A:TYR169 5.0 32.9 1.0
C A:ARG164 5.0 23.5 1.0

Chlorine binding site 2 out of 5 in 7ly8

Go back to Chlorine Binding Sites List in 7ly8
Chlorine binding site 2 out of 5 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl409

b:65.2
occ:1.00
 O B:HOH674 4.0 23.6 1.0
O B:HOH567 4.1 33.5 1.0
O B:HOH781 4.2 28.8 1.0
O B:HOH831 4.4 27.7 1.0
O1 B:PEG403 4.6 29.3 1.0
O B:HOH836 4.6 23.1 1.0
O B:HOH892 4.8 34.4 1.0
O B:HOH530 4.9 17.0 1.0
O B:HOH613 4.9 26.7 1.0

Chlorine binding site 3 out of 5 in 7ly8

Go back to Chlorine Binding Sites List in 7ly8
Chlorine binding site 3 out of 5 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl410

b:66.5
occ:1.00
 O B:HOH836 4.4 23.1 1.0
O B:HOH832 4.6 41.0 1.0
O B:HOH802 4.7 21.2 1.0
O B:HOH526 4.7 21.7 1.0
O B:HOH874 4.7 31.2 1.0
O B:HOH604 4.8 16.5 1.0
O B:HOH886 4.9 30.7 1.0
O B:HOH872 5.0 23.4 1.0

Chlorine binding site 4 out of 5 in 7ly8

Go back to Chlorine Binding Sites List in 7ly8
Chlorine binding site 4 out of 5 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl411

b:64.6
occ:1.00
 O B:HOH621 4.2 33.6 1.0
O B:HOH593 4.4 22.0 1.0

Chlorine binding site 5 out of 5 in 7ly8

Go back to Chlorine Binding Sites List in 7ly8
Chlorine binding site 5 out of 5 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'- Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl412

b:73.6
occ:1.00
 O B:HOH591 3.7 48.7 1.0
N B:GLY221 4.0 15.5 1.0
C B:GLU220 4.0 16.2 1.0
O B:LYS219 4.1 16.8 1.0
O B:ASP218 4.2 18.4 1.0
CA B:GLY221 4.3 16.3 1.0
C B:LYS219 4.3 16.5 1.0
O B:GLU220 4.4 16.9 1.0
CA B:GLU220 4.5 15.8 1.0
N B:GLU220 4.5 15.8 1.0
O B:LEU217 4.9 16.3 1.0

Reference:

E.Hilario, M.F.Dunn, L.J.Mueller. The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Two Molecules of N-(4'-Trifluoromethoxybenzoyl)-2-Amino-1-Ethylphosphate (F6F) Inhibitor at the Enzyme Alpha-Site, A Single F6F Molecule at the Enzyme Beta-Site, and Sodium Ion at the Metal Coordination Site at 1.55 Angstrom Resolution. One of the Beta-Q114 Rotamer Conformations Allows A Hydrogen Bond to Form with the Plp Oxygen at the Position 3 in the Ring. To Be Published.
Page generated: Tue Apr 4 20:45:51 2023

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