Fluorine 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:

Caesium (Cs) 2 atoms
Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine 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 Fluorine atom.
In total 3 binding sites of Fluorine 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 Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 7jmq

Go back to Fluorine Binding Sites List in 7jmq
Fluorine binding site 1 out of 3 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 Fluorine with other atoms in the F 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:F308

b:11.6
occ:1.00
F9F A:F9F308 0.0 11.6 1.0
C8 A:F9F308 1.3 12.2 1.0
F10 A:F9F308 2.1 11.9 1.0
O7 A:F9F308 2.1 11.8 1.0
F11 A:F9F308 2.1 12.5 1.0
O A:HOH658 3.2 11.9 1.0
O A:HOH534 3.2 10.3 1.0
O A:ALA129 3.2 9.9 1.0
O B:HOH730 3.4 8.3 1.0
C1 A:F9F308 3.5 11.6 1.0
CB B:PRO18 3.5 9.6 1.0
CB A:ALA59 3.7 10.6 1.0
CG B:PRO18 4.0 9.6 1.0
O A:HOH562 4.1 16.6 1.0
CB A:ALA129 4.1 8.8 1.0
C A:ALA129 4.1 9.0 1.0
C2 A:F9F308 4.1 12.1 1.0
CA A:ALA129 4.2 8.6 1.0
CA B:PRO18 4.2 9.5 1.0
C6 A:F9F308 4.5 11.8 1.0
CZ A:PHE212 4.8 10.0 1.0
CD1 A:ILE153 4.9 12.8 1.0
CG1 A:ILE153 4.9 12.4 1.0
N B:GLN19 5.0 9.5 1.0

Fluorine binding site 2 out of 3 in 7jmq

Go back to Fluorine Binding Sites List in 7jmq
Fluorine binding site 2 out of 3 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 Fluorine with other atoms in the F 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
A:F308

b:11.9
occ:1.00
F10 A:F9F308 0.0 11.9 1.0
C8 A:F9F308 1.3 12.2 1.0
F9F A:F9F308 2.1 11.6 1.0
F11 A:F9F308 2.1 12.5 1.0
O7 A:F9F308 2.2 11.8 1.0
C1 A:F9F308 2.9 11.6 1.0
C2 A:F9F308 3.0 12.1 1.0
O A:HOH534 3.2 10.3 1.0
CA A:ALA129 3.4 8.6 1.0
CD1 A:ILE153 3.5 12.8 1.0
O A:ALA129 3.5 9.9 1.0
CD2 A:LEU127 3.5 8.6 1.0
CB A:ALA129 3.5 8.8 1.0
CG1 A:ILE153 3.7 12.4 1.0
C A:ALA129 3.9 9.0 1.0
C6 A:F9F308 4.1 11.8 1.0
C3 A:F9F308 4.2 12.2 1.0
O A:HOH475 4.3 16.1 1.0
O B:HOH730 4.5 8.3 1.0
N A:ALA129 4.5 8.2 1.0
CG A:LEU127 4.7 8.5 1.0
CD1 A:LEU127 4.8 8.8 1.0
O A:HOH658 4.8 11.9 1.0
O A:VAL128 4.9 8.4 1.0
CB A:ILE153 5.0 12.0 1.0

Fluorine binding site 3 out of 3 in 7jmq

Go back to Fluorine Binding Sites List in 7jmq
Fluorine binding site 3 out of 3 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 Fluorine with other atoms in the F binding site number 3 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:F308

b:12.5
occ:1.00
F11 A:F9F308 0.0 12.5 1.0
C8 A:F9F308 1.3 12.2 1.0
F10 A:F9F308 2.1 11.9 1.0
F9F A:F9F308 2.1 11.6 1.0
O7 A:F9F308 2.2 11.8 1.0
C1 A:F9F308 2.9 11.6 1.0
C2 A:F9F308 2.9 12.1 1.0
O A:HOH658 3.2 11.9 1.0
CD1 A:ILE153 3.4 12.8 1.0
O B:HOH730 3.6 8.3 1.0
CZ A:PHE212 3.7 10.0 1.0
CG1 A:ILE153 3.9 12.4 1.0
CD2 A:LEU177 4.0 12.6 1.0
CE1 A:PHE212 4.0 9.9 1.0
O A:HOH534 4.0 10.3 1.0
C6 A:F9F308 4.2 11.8 1.0
C3 A:F9F308 4.2 12.2 1.0
CG A:LEU177 4.4 13.3 1.0
CD1 A:LEU177 4.5 12.8 1.0
CG2 A:ILE153 4.5 12.1 1.0
CE2 A:PHE212 4.7 9.8 1.0
CB A:ILE153 4.8 12.0 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 13:47:56 2021

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