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Atomistry » Caesium » PDB 7jqw-8u8l » 7lkl | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Caesium » PDB 7jqw-8u8l » 7lkl » |
Caesium 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 RingEnzymatic 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:
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 Binding Sites:
The binding sites of Caesium 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 Caesium atom.
In total 8 binding sites of Caesium 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 Caesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; Caesium binding site 1 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 1 out
of 8 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
Caesium binding site 2 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 2 out
of 8 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
Caesium binding site 3 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 3 out
of 8 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
Caesium binding site 4 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 4 out
of 8 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
Caesium binding site 5 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 5 out
of 8 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
Caesium binding site 6 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 6 out
of 8 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
Caesium binding site 7 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 7 out
of 8 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
Caesium binding site 8 out of 8 in 7lklGo back to Caesium Binding Sites List in 7lkl
Caesium binding site 8 out
of 8 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
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.
Page generated: Tue Jul 30 21:16:06 2024
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