Caesium in PDB 7jmq: The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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 External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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 External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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 External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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: 7jmq 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)*	38.86 / 1.60
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	181.38, 58.244, 67.154, 90, 94.33, 90
*R / R_free (%)*	15.8 / 18.4

Other elements in 7jmq:

The structure of The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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:

Chlorine	(Cl)	1 atom
Sodium	(Na)	1 atom
Fluorine	(F)	3 atoms

Caesium Binding Sites:

The binding sites of Caesium atom in the The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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 7jmq). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 2 binding sites of Caesium where determined in the The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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: 7jmq:
Jump to Caesium binding site number: 1; 2;

Caesium binding site 1 out of 2 in 7jmq

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Caesium Binding Sites List in 7jmq

Caesium binding site 1 out of 2 in the The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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 Caesium with other atoms in the Cs binding site number 1 of The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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:Cs313 b:22.6 occ:0.46	O	A:ALA167	2.9	16.4	1.0
	O	A:HOH630	3.1	48.3	1.0
	O	A:GLY170	3.2	14.0	1.0
	O	A:HOH678	3.2	33.6	1.0
	O	A:HIS204	3.5	16.2	1.0
	N	A:ALA206	4.0	12.3	1.0
	C	A:ALA167	4.1	16.0	1.0
	O	A:SER168	4.2	16.6	0.5
	C	A:GLY170	4.2	13.7	1.0
	O	A:HOH503	4.2	40.4	1.0
	O	A:HOH565	4.3	13.5	0.6
	C	A:ALA205	4.3	13.2	1.0
	CA	A:ALA205	4.3	13.8	1.0
	NH2	A:ARG171	4.4	18.0	1.0
	O	A:SER168	4.5	16.5	0.5
	CD	A:ARG171	4.5	16.0	1.0
	C	A:HIS204	4.6	16.4	1.0
	C	A:SER168	4.7	16.6	0.5
	C	A:SER168	4.8	16.5	0.5
	CA	A:ALA206	4.8	11.9	1.0
	CB	A:ALA206	4.9	11.8	1.0
	N	A:GLY170	4.9	14.3	1.0
	N	A:ALA205	4.9	15.0	1.0
	CA	A:SER168	5.0	16.3	0.5
	CA	A:SER168	5.0	16.6	0.5

Caesium binding site 2 out of 2 in 7jmq

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Caesium Binding Sites List in 7jmq

Caesium binding site 2 out of 2 in the The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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 Caesium with other atoms in the Cs binding site number 2 of The External Aldimine Form of the Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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:Cs428 b:12.9 occ:0.69	O	B:THR71	3.0	10.0	1.0
	O	B:THR69	3.1	13.6	1.0
	O	B:HOH625	3.2	23.2	1.0
	O	B:HOH817	3.2	37.5	1.0
	O	B:THR66	3.3	12.3	1.0
	OG1	B:THR66	3.3	11.8	1.0
	O	B:HOH744	3.5	35.5	1.0
	CB	B:THR66	3.9	11.8	1.0
	C	B:THR66	3.9	12.8	1.0
	O	B:HOH862	3.9	22.2	1.0
	C	B:THR69	4.1	13.1	1.0
	C	B:THR71	4.1	9.4	1.0
	OG1	B:THR69	4.3	11.5	1.0
	N	B:THR71	4.5	10.0	1.0
	N	B:ALA67	4.6	13.4	1.0
	CA	B:THR66	4.6	12.3	1.0
	N	B:THR69	4.6	14.3	1.0
	CA	B:ALA67	4.6	14.4	1.0
	O	B:HOH637	4.7	10.5	1.0
	O	B:HOH812	4.8	45.2	0.6
	N	B:GLY68	4.9	15.9	1.0
	CA	B:ARG70	4.9	12.8	1.0
	N	B:ARG70	4.9	13.0	1.0
	C	B:ARG70	4.9	12.0	1.0
	CA	B:THR69	4.9	13.3	1.0
	OG1	B:THR72	5.0	10.1	1.0
	CA	B:THR71	5.0	9.6	1.0
	N	B:THR72	5.0	9.3	1.0

Reference:

E.Hilario, M.F.Dunn, L.J.Mueller. The External Aldimine Form of Mutant Beta-S377A Salmonella Thypi Tryptophan Synthase in Open Conformation Showing Dual Side Chain Conformations For the Residue Beta-Q114, Sodium Ion at the Metal Coordination Site, and F9 Inhibitor at the Alpha-Site. 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.

Page generated: Tue Jul 30 21:08:17 2024

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