Sodium in PDB 7l03: 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 Sodium Ion at the Metal Coordination Site at 1.60 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 Sodium Ion at the Metal Coordination Site at 1.60 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 Sodium Ion at the Metal Coordination Site at 1.60 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 Sodium Ion at the Metal Coordination Site at 1.60 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site, PDB code: 7l03 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)*	39.24 / 1.60
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	182.49, 59.05, 67.245, 90, 95.02, 90
*R / R_free (%)*	17.1 / 22.4

Other elements in 7l03:

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 Sodium Ion at the Metal Coordination Site at 1.60 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

Sodium Binding Sites:

The binding sites of Sodium 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 Sodium Ion at the Metal Coordination Site at 1.60 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site (pdb code 7l03). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was 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 Sodium Ion at the Metal Coordination Site at 1.60 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site, PDB code: 7l03:

Sodium binding site 1 out of 1 in 7l03

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Sodium Binding Sites List in 7l03

Sodium binding site 1 out of 1 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 Sodium Ion at the Metal Coordination Site at 1.60 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 Sodium with other atoms in the Na 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 Sodium Ion at the Metal Coordination Site at 1.60 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:Na505 b:28.9 occ:1.00	OE2	B:GLU256	2.6	15.4	1.0
	O	B:HOH678	2.9	28.6	1.0
	O	B:GLY232	3.0	19.1	1.0
	O	B:VAL231	3.2	13.9	1.0
	O	B:SER308	3.4	15.6	1.0
	O	B:GLY268	3.5	14.3	1.0
	CD	B:GLU256	3.6	14.7	1.0
	CD	B:PRO270	3.7	15.7	1.0
	CG	B:GLU256	3.7	13.6	1.0
	C	B:GLY232	3.8	15.9	1.0
	CG	B:PRO270	3.9	16.5	1.0
	CB	B:VAL309	3.9	13.0	1.0
	CG2	B:VAL309	4.0	15.0	1.0
	C	B:VAL231	4.0	12.5	1.0
	CG1	B:VAL231	4.0	13.3	1.0
	CA	B:GLY232	4.1	13.5	1.0
	CB	B:GLU256	4.4	11.9	1.0
	C	B:SER308	4.4	14.3	1.0
	N	B:GLY232	4.5	12.6	1.0
	CA	B:VAL309	4.5	12.8	1.0
	O	B:PHE306	4.6	20.2	1.0
	C	B:GLY268	4.6	14.4	1.0
	CB	B:VAL231	4.7	11.3	1.0
	N	B:PRO270	4.7	15.2	1.0
	OE1	B:GLU256	4.7	15.5	1.0
	CD	B:PRO257	4.8	11.8	1.0
	CA	B:ALA269	4.9	13.2	1.0
	N	B:VAL309	4.9	13.9	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 Sodium Ion at the Metal Coordination Site at 1.60 Angstrom Resolution. Three Water Molecules Are Close to the Amynoacrylate at the Enzyme Beta-Site. To Be Published.

Page generated: Tue Oct 8 17:31:26 2024

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