Fluorine in PDB 7lkl: The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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: 7lkl 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) 28.92 / 1.05
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 181.741, 59.81, 67.299, 90, 94.65, 90
R / Rfree (%) 15.5 / 17.6

Other elements in 7lkl:

The structure of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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:

Caesium (Cs) 8 atoms
Chlorine (Cl) 4 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 7lkl). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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: 7lkl:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 7lkl

Go back to Fluorine Binding Sites List in 7lkl
Fluorine binding site 1 out of 3 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 Fluorine with other atoms in the F binding site number 1 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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:F301

b:11.8
occ:0.95
 F9F A:F9F301 0.0 11.8 0.9
C8 A:F9F301 1.3 10.5 0.9
O7 A:F9F301 2.1 11.1 0.9
F10 A:F9F301 2.1 11.5 0.9
F11 A:F9F301 2.1 12.8 0.9
O A:HOH554 3.1 9.4 1.0
O A:HOH691 3.1 11.7 1.0
O B:HOH857 3.3 9.8 1.0
O A:ALA129 3.3 9.7 1.0
CB B:PRO18 3.4 9.7 1.0
C1 A:F9F301 3.5 9.9 0.9
CB A:ALA59 3.6 12.6 1.0
O A:HOH551 4.0 15.4 1.0
CB A:ALA129 4.0 10.5 1.0
CG B:PRO18 4.1 10.4 1.0
C A:ALA129 4.1 8.7 1.0
C6 A:F9F301 4.2 10.2 0.9
CA A:ALA129 4.2 9.1 1.0
CA B:PRO18 4.3 8.2 1.0
C2 A:F9F301 4.5 10.3 0.9
CZ A:PHE212 4.8 11.9 1.0
CG1 A:ILE153 4.8 13.2 1.0
CD1 A:ILE153 4.9 15.8 1.0
N B:GLN19 4.9 8.3 1.0
CA A:ALA59 5.0 11.2 1.0

Fluorine binding site 2 out of 3 in 7lkl

Go back to Fluorine Binding Sites List in 7lkl
Fluorine binding site 2 out of 3 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 Fluorine with other atoms in the F binding site number 2 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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:F301

b:11.5
occ:0.95
 F10 A:F9F301 0.0 11.5 0.9
C8 A:F9F301 1.3 10.5 0.9
F9F A:F9F301 2.1 11.8 0.9
F11 A:F9F301 2.2 12.8 0.9
O7 A:F9F301 2.2 11.1 0.9
C1 A:F9F301 2.9 9.9 0.9
C6 A:F9F301 3.0 10.2 0.9
O A:HOH554 3.2 9.4 1.0
CA A:ALA129 3.4 9.1 1.0
CD2 A:LEU127 3.4 9.7 1.0
CD1 A:ILE153 3.4 15.8 1.0
CB A:ALA129 3.5 10.5 1.0
O A:ALA129 3.6 9.7 1.0
CG1 A:ILE153 3.7 13.2 1.0
C A:ALA129 4.0 8.7 1.0
C2 A:F9F301 4.1 10.3 0.9
C5 A:F9F301 4.3 9.6 0.9
O B:HOH857 4.4 9.8 1.0
O A:HOH474 4.4 17.4 1.0
N A:ALA129 4.5 8.3 1.0
CG A:LEU127 4.6 9.0 1.0
CD1 A:LEU127 4.7 10.3 1.0
O A:HOH691 4.8 11.7 1.0
CB A:ALA59 4.9 12.6 1.0
CB A:ILE153 5.0 11.1 1.0
O A:VAL128 5.0 8.3 1.0

Fluorine binding site 3 out of 3 in 7lkl

Go back to Fluorine Binding Sites List in 7lkl
Fluorine binding site 3 out of 3 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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 Fluorine with other atoms in the F binding site number 3 of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Inhibitor N-(4'- Trifluoromethoxybenzenesulfonyl)-2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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:F301

b:12.8
occ:0.95
 F11 A:F9F301 0.0 12.8 0.9
C8 A:F9F301 1.3 10.5 0.9
F9F A:F9F301 2.1 11.8 0.9
F10 A:F9F301 2.2 11.5 0.9
O7 A:F9F301 2.2 11.1 0.9
C1 A:F9F301 2.9 9.9 0.9
C6 A:F9F301 2.9 10.2 0.9
O A:HOH691 3.1 11.7 1.0
CD1 A:ILE153 3.4 15.8 1.0
O B:HOH857 3.5 9.8 1.0
CZ A:PHE212 3.8 11.9 1.0
CG1 A:ILE153 3.9 13.2 1.0
O A:HOH554 3.9 9.4 1.0
CD2 A:LEU177 4.0 17.1 1.0
CE1 A:PHE212 4.1 11.6 1.0
C2 A:F9F301 4.2 10.3 0.9
C5 A:F9F301 4.2 9.6 0.9
CG2 A:ILE153 4.3 12.8 1.0
CG A:LEU177 4.4 17.1 1.0
CD1 A:LEU177 4.5 16.4 1.0
CB A:ILE153 4.7 11.1 1.0
CE2 A:PHE212 4.7 11.2 1.0
O A:HOH551 4.9 15.4 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 Inhibitor N-(4'-Trifluoromethoxybenzenesulfonyl) -2-Amino-1-Ethylphosphate (F9F) at the Enzyme Alpha-Site, Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.05 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.
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