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Caesium in PDB 7l1h: The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site

Enzymatic activity of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site

All present enzymatic activity of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site:
4.2.1.20;

Protein crystallography data

The structure of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site, PDB code: 7l1h 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) 39.40 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.97, 59.73, 67.42, 90, 94.7, 90
R / Rfree (%) 13.8 / 18.5

Other elements in 7l1h:

The structure of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Chlorine (Cl) 7 atoms

Caesium Binding Sites:

The binding sites of Caesium atom in the The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site (pdb code 7l1h). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 4 binding sites of Caesium where determined in the The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site, PDB code: 7l1h:
Jump to Caesium binding site number: 1; 2; 3; 4;

Caesium binding site 1 out of 4 in 7l1h

Go back to Caesium Binding Sites List in 7l1h
Caesium binding site 1 out of 4 in the The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs415

b:24.6
occ:0.50
CS B:CS415 0.0 24.6 0.5
CS B:CS415 2.7 97.9 0.5
O B:THR71 3.0 14.5 1.0
O B:HOH668 3.1 46.9 1.0
O B:THR69 3.2 17.6 1.0
O B:THR66 3.2 17.7 1.0
OG1 B:THR66 3.3 19.2 1.0
O B:HOH835 3.4 63.2 1.0
O B:HOH921 3.7 40.2 1.0
CB B:THR66 3.8 15.8 1.0
C B:THR66 4.0 16.1 1.0
C B:THR71 4.1 14.2 1.0
C B:THR69 4.2 16.1 1.0
OG1 B:THR69 4.2 14.1 1.0
O B:HOH757 4.4 48.0 1.0
N B:THR71 4.5 13.8 1.0
CA B:THR66 4.6 15.2 1.0
N B:THR69 4.6 17.5 1.0
N B:ALA67 4.7 16.7 1.0
O B:HOH632 4.7 16.4 1.0
CA B:ALA67 4.8 18.4 1.0
C B:ARG70 4.9 14.0 1.0
N B:THR72 4.9 13.7 1.0
CA B:THR69 4.9 15.4 1.0
CA B:THR71 4.9 12.5 1.0
N B:ARG70 5.0 13.8 1.0
CA B:ARG70 5.0 14.1 0.5
CA B:ARG70 5.0 14.2 0.5

Caesium binding site 2 out of 4 in 7l1h

Go back to Caesium Binding Sites List in 7l1h
Caesium binding site 2 out of 4 in the The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 2 of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs415

b:97.9
occ:0.50
CS B:CS415 0.0 97.9 0.5
CS B:CS415 2.7 24.6 0.5
O B:HOH503 3.7 49.3 1.0
O B:THR69 3.7 17.6 1.0
OG1 B:THR72 4.1 17.0 1.0
O B:THR71 4.2 14.5 1.0
CZ B:ARG70 4.3 26.4 0.5
O B:HOH655 4.3 18.9 0.9
NH1 B:ARG70 4.3 29.9 0.5
O B:HOH921 4.4 40.2 1.0
O B:HOH554 4.4 36.5 0.9
O B:HOH757 4.4 48.0 1.0
CA B:ARG70 4.4 14.1 0.5
CA B:ARG70 4.4 14.2 0.5
O B:HOH835 4.5 63.2 1.0
NH2 B:ARG70 4.5 30.6 0.5
C B:ARG70 4.5 14.0 1.0
NE B:ARG70 4.7 23.5 0.5
C B:THR71 4.7 14.2 1.0
C B:THR69 4.7 16.1 1.0
O B:ARG70 4.8 15.1 1.0
N B:THR71 4.8 13.8 1.0

Caesium binding site 3 out of 4 in 7l1h

Go back to Caesium Binding Sites List in 7l1h
Caesium binding site 3 out of 4 in the The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 3 of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs416

b:17.2
occ:0.60
CS B:CS416 0.0 17.2 0.6
CS B:CS416 1.9 15.4 0.4
O B:PHE306 2.9 15.9 1.0
O B:GLY268 3.1 11.6 1.0
O B:SER308 3.2 14.7 1.0
O B:GLY232 3.3 16.3 1.0
O B:LEU304 3.5 15.0 1.0
O B:VAL231 3.7 14.1 1.0
C B:GLY232 3.8 15.2 1.0
CA B:GLY232 3.8 13.8 1.0
C B:PHE306 4.0 14.4 1.0
C B:GLY268 4.1 12.5 1.0
CD B:PRO270 4.2 13.7 1.0
CB B:PHE306 4.2 17.4 1.0
CD B:PRO257 4.3 10.8 1.0
N B:PHE306 4.4 14.8 1.0
C B:SER308 4.4 12.2 1.0
CA B:PHE306 4.5 15.5 1.0
C B:LEU304 4.6 13.0 1.0
CG B:PRO270 4.6 15.0 1.0
C B:VAL231 4.6 12.9 1.0
CG B:PRO257 4.6 12.1 1.0
CA B:GLY268 4.6 12.5 1.0
CD2 B:PHE306 4.6 18.4 1.0
N B:GLY232 4.7 12.8 1.0
N B:SER308 4.8 13.2 1.0
OE2 B:GLU256 4.9 14.3 1.0
N B:GLY233 4.9 13.1 1.0
CG B:PHE306 5.0 18.2 1.0

Caesium binding site 4 out of 4 in 7l1h

Go back to Caesium Binding Sites List in 7l1h
Caesium binding site 4 out of 4 in the The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 4 of The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs416

b:15.4
occ:0.40
CS B:CS416 0.0 15.4 0.4
CS B:CS416 1.9 17.2 0.6
O B:GLY232 3.1 16.3 1.0
O B:VAL231 3.2 14.1 1.0
OE2 B:GLU256 3.3 14.3 1.0
O B:GLY268 3.3 11.6 1.0
O B:SER308 3.3 14.7 1.0
CD B:PRO270 3.8 13.7 1.0
C B:GLY232 4.0 15.2 1.0
CB B:VAL309 4.0 12.7 1.0
CG2 B:VAL309 4.1 14.2 1.0
CG B:PRO270 4.1 15.0 1.0
C B:VAL231 4.1 12.9 1.0
CD B:GLU256 4.2 13.6 1.0
CG B:GLU256 4.2 14.0 1.0
CA B:GLY232 4.2 13.8 1.0
CG1 B:VAL231 4.2 14.6 1.0
C B:SER308 4.4 12.2 1.0
C B:GLY268 4.5 12.5 1.0
O B:PHE306 4.5 15.9 1.0
CB B:GLU256 4.5 12.0 1.0
CD B:PRO257 4.6 10.8 1.0
CA B:VAL309 4.6 12.0 1.0
N B:GLY232 4.6 12.8 1.0
CB B:VAL231 4.7 12.0 1.0
N B:PRO270 4.9 12.6 1.0
N B:VAL309 4.9 11.6 1.0
CA B:ALA269 5.0 12.2 1.0

Reference:

E.Hilario, M.F.Dunn, L.J.Mueller. The Aminoacrylate 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 and Cesium Ion at the Metal Coordination Site at 1.50 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site To Be Published.
Page generated: Thu Mar 31 02:41:50 2022

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