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

Protein crystallography data

Other elements in 7lkl:

Fluorine Binding Sites:

Fluorine binding site 1 out of 3 in 7lkl

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

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

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

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