Chlorine 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

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:

*Resolution Low / High (Å)*	28.92 / 1.05
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	181.741, 59.81, 67.299, 90, 94.65, 90
*R / R_free (%)*	15.5 / 17.6

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:

Fluorine	(F)	3 atoms
Caesium	(Cs)	8 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 1.05 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 Chlorine atom.
In total 4 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 1.05 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 Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 7lkl

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Chlorine Binding Sites List in 7lkl

Chlorine binding site 1 out of 4 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 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 1.05 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:Cl312 b:31.9 occ:1.00	O	A:HOH667	2.7	33.3	1.0
	N	A:TYR4	2.9	8.9	1.0
	O	A:HOH622	2.9	34.2	1.0
	N	A:ARG3	3.1	11.4	1.0
	O	A:HOH418	3.3	13.5	1.0
	C	A:GLU2	3.4	16.0	1.0
	CB	A:TYR4	3.5	9.8	1.0
	CD2	A:TYR4	3.6	8.6	1.0
	CA	A:TYR4	3.7	9.4	1.0
	CA	A:GLU2	3.7	21.4	1.0
	C	A:ARG3	3.8	8.4	1.0
	N	A:GLU5	3.9	10.1	1.0
	CA	A:ARG3	4.0	9.7	1.0
	CG	A:TYR4	4.0	8.9	1.0
	O	A:GLU2	4.1	14.4	1.0
	O	A:HOH628	4.2	25.4	1.0
	O	A:MET1	4.3	27.8	1.0
	C	A:TYR4	4.3	9.7	1.0
	O	A:HOH532	4.5	14.8	1.0
	N	A:GLU2	4.5	22.3	1.0
	CB	A:ARG3	4.6	8.6	1.0
	OE2	A:GLU5	4.7	35.9	1.0
	CE2	A:TYR4	4.7	9.1	1.0
	CG	A:GLU5	4.7	18.4	1.0
	C	A:MET1	4.7	23.3	1.0
	CD	A:GLU5	4.8	25.4	1.0
	CB	A:GLU2	4.9	25.2	1.0
	CB	A:ASP124	4.9	8.1	1.0
	CA	A:GLY172	5.0	9.6	1.0
	O	A:ARG3	5.0	8.5	1.0

Chlorine binding site 2 out of 4 in 7lkl

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Chlorine Binding Sites List in 7lkl

Chlorine binding site 2 out of 4 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 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 1.05 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
B:Cl524 b:32.0 occ:1.00	OD2	B:ASP323	3.0	15.2	1.0
	O	B:HOH1011	3.8	33.1	1.0
	O	B:HOH866	3.8	45.8	1.0
	CG	B:ASP323	3.9	10.4	1.0
	O	B:HOH772	4.0	20.3	1.0
	O	B:HOH779	4.1	12.2	1.0
	OD1	B:ASP323	4.1	11.3	1.0
	O	B:HOH914	4.8	33.6	1.0
	O	B:HOH1022	4.9	17.5	1.0
	O	B:GLY320	5.0	9.1	1.0

Chlorine binding site 3 out of 4 in 7lkl

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Chlorine Binding Sites List in 7lkl

Chlorine binding site 3 out of 4 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 Chlorine with other atoms in the Cl 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
B:Cl525 b:54.4 occ:1.00	O	B:ARG141	3.4	19.3	1.0
	O	B:HOH980	3.6	45.2	1.0
	CD	B:PRO144	3.9	15.8	1.0
	O	B:HOH789	4.0	16.4	1.0
	CG	B:PRO144	4.0	15.7	1.0
	OE1	B:GLN142	4.0	16.1	1.0
	O	B:HOH757	4.2	52.8	1.0
	O	B:HOH618	4.4	25.6	1.0
	C	B:ARG141	4.6	15.9	1.0
	CA	B:GLN142	4.6	13.4	1.0
	O	B:HOH669	4.8	29.5	1.0
	O	B:LYS382	4.8	20.3	1.0
	CD	B:GLN142	4.9	14.7	1.0

Chlorine binding site 4 out of 4 in 7lkl

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Chlorine Binding Sites List in 7lkl

Chlorine binding site 4 out of 4 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 Chlorine with other atoms in the Cl binding site number 4 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
B:Cl526 b:55.5 occ:1.00	O	B:HOH740	3.6	18.1	1.0
	CG	B:TYR8	3.6	8.2	1.0
	CD1	B:TYR8	3.6	8.9	1.0
	CD2	B:TYR8	3.7	8.9	1.0
	CE1	B:TYR8	3.8	9.6	1.0
	O	B:HOH1042	3.9	44.4	1.0
	CE2	B:TYR8	3.9	9.4	1.0
	CZ	B:TYR8	3.9	9.8	1.0
	O	B:GLY10	4.0	11.1	1.0
	O	B:HOH675	4.1	26.2	1.0
	O	B:HOH674	4.2	23.0	1.0
	CB	B:TYR8	4.3	7.9	1.0
	O	B:HOH676	4.4	27.4	1.0
	CA	B:GLU11	4.7	10.3	1.0
	OH	B:TYR8	4.7	12.5	1.0
	O	B:GLU11	4.9	9.4	1.0
	C	B:GLY10	5.0	9.4	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 1.05 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.

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