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 / R_free (%)*	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

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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

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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

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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

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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.

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