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 / Rfree (%) 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

Go back to 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

Go back to 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: Sat Aug 21 13:29:05 2021

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