Chlorine in PDB 7ltp: 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 1.47 Angstrom Resolution

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 1.47 Angstrom Resolution

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 1.47 Angstrom Resolution:
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 1.47 Angstrom Resolution, PDB code: 7ltp 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)*	39.16 / 1.47
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	182.414, 59.223, 67.186, 90, 94.84, 90
*R / R_free (%)*	13.3 / 16.7

Other elements in 7ltp:

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 1.47 Angstrom Resolution also contains other interesting chemical elements:

Caesium	(Cs)	5 atoms
Fluorine	(F)	3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 1.47 Angstrom Resolution (pdb code 7ltp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine 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 1.47 Angstrom Resolution, PDB code: 7ltp:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7ltp

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Chlorine Binding Sites List in 7ltp

Chlorine binding site 1 out of 2 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 1.47 Angstrom Resolution

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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 1.47 Angstrom Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl412 b:72.2 occ:1.00	O	B:HOH864	3.9	30.3	1.0
	O	B:HOH538	4.0	36.5	1.0
	O	B:HOH810	4.1	34.9	1.0
	O	B:HOH603	4.3	21.6	1.0
	O	B:HOH524	4.5	19.2	1.0
	O	B:HOH865	4.7	33.5	1.0
	O1	B:PEG406	4.8	30.5	1.0
	O	B:HOH931	5.0	46.9	1.0
	O	B:HOH887	5.0	51.0	1.0

Chlorine binding site 2 out of 2 in 7ltp

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Chlorine Binding Sites List in 7ltp

Chlorine binding site 2 out of 2 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 1.47 Angstrom Resolution

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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 1.47 Angstrom Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl413 b:61.0 occ:1.00	O	B:HOH803	2.6	28.1	1.0
	S	B:DMS409	3.4	48.5	1.0
	O	B:DMS409	3.6	53.3	1.0
	OE2	B:GLU263	3.6	28.1	1.0
	C1	B:DMS409	3.8	30.8	1.0
	O	B:HIS260	3.9	16.3	1.0
	CA	B:GLY261	4.2	13.9	1.0
	CG2	B:THR328	4.3	12.1	1.0
	CD	B:GLU263	4.5	26.3	1.0
	OE1	B:GLU263	4.6	25.6	1.0
	C	B:HIS260	4.7	13.8	1.0
	N	B:GLY261	4.8	13.0	1.0
	O	B:HOH621	4.8	39.7	1.0
	O	B:HOH742	5.0	16.0	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 1.47 Angstrom Resolution. To Be Published.

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