Atomistry » Caesium » PDB 7jqw-8rsy » 7lkl
Atomistry »
  Caesium »
    PDB 7jqw-8rsy »
      7lkl »

Caesium 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 / Rfree (%) 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
Chlorine (Cl) 4 atoms

Caesium Binding Sites:

The binding sites of Caesium 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 Caesium atom.
In total 8 binding sites of Caesium 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 Caesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Caesium binding site 1 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 1 out of 8 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 Caesium with other atoms in the Cs 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:Cs310

b:19.0
occ:0.70
 CS A:CS310 0.0 19.0 0.7
CS A:CS310 1.3 31.5 0.3
O A:ALA167 3.0 16.4 1.0
O A:HOH672 3.1 47.5 1.0
O A:GLY170 3.2 17.2 1.0
O A:HIS204 3.4 16.5 1.0
O A:HOH611 3.4 36.3 1.0
O A:HOH518 3.4 30.3 1.0
O A:HOH704 3.4 30.8 1.0
N A:ALA206 3.9 11.5 1.0
C A:ALA205 4.2 11.4 1.0
C A:ALA167 4.2 13.8 1.0
CA A:ALA205 4.3 11.9 1.0
C A:GLY170 4.3 13.8 1.0
O A:SER168 4.3 17.4 1.0
O A:HOH603 4.4 56.4 1.0
C A:HIS204 4.4 14.8 1.0
CD A:ARG171 4.5 17.2 1.0
O A:HOH643 4.5 41.6 1.0
O A:HOH610 4.6 46.2 1.0
NH2 A:ARG171 4.6 20.1 1.0
CA A:ALA206 4.7 10.8 1.0
C A:SER168 4.8 15.5 1.0
CB A:ALA206 4.8 10.7 1.0
N A:ALA205 4.8 13.7 1.0

Caesium binding site 2 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 2 out of 8 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 Caesium with other atoms in the Cs 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
A:Cs310

b:31.5
occ:0.30
 CS A:CS310 0.0 31.5 0.3
CS A:CS310 1.3 19.0 0.7
O A:ALA167 3.0 16.4 1.0
O A:HOH611 3.1 36.3 1.0
O A:HOH672 3.1 47.5 1.0
O A:GLY170 3.2 17.2 1.0
O A:SER168 3.3 17.4 1.0
O A:HOH610 3.3 46.2 1.0
NH2 A:ARG171 3.7 20.1 1.0
O A:HOH643 3.8 41.6 1.0
C A:SER168 3.9 15.5 1.0
O A:HIS204 4.1 16.5 1.0
O A:HOH518 4.1 30.3 1.0
C A:ALA167 4.1 13.8 1.0
CA A:SER168 4.2 15.7 1.0
CZ A:ARG171 4.3 19.7 1.0
O A:HOH704 4.3 30.8 1.0
CD A:ARG171 4.3 17.2 1.0
C A:GLY170 4.4 13.8 1.0
NE A:ARG171 4.5 19.9 1.0
N A:SER168 4.7 14.1 1.0
N A:GLY170 4.8 14.5 1.0
N A:TYR169 4.9 13.4 1.0

Caesium binding site 3 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 3 out of 8 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 Caesium with other atoms in the Cs 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
A:Cs311

b:16.2
occ:0.90
 CS A:CS311 0.0 16.2 0.9
CS A:CS311 1.5 11.6 0.1
O A:ALA265 3.1 12.6 1.0
OG A:SER221 3.2 12.6 0.7
O A:ARG267 3.3 19.0 1.0
O A:HOH525 3.4 25.0 1.0
O A:HOH547 3.5 30.9 1.0
O A:HOH676 3.6 34.3 1.0
O A:HOH466 3.8 45.3 1.0
CB A:SER221 3.9 9.4 0.3
C A:ALA265 4.1 10.5 1.0
CB A:SER221 4.1 11.2 0.7
O A:HOH590 4.2 45.2 1.0
C A:ARG267 4.4 18.0 1.0
CA A:SER221 4.5 9.7 0.3
CA A:SER221 4.6 10.3 0.7
N A:ARG267 4.7 13.7 1.0
C A:SER266 4.8 12.3 1.0
CA A:ALA265 4.8 10.8 1.0
O A:HOH458 4.9 23.8 1.0
N A:SER266 4.9 10.5 1.0

Caesium binding site 4 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 4 out of 8 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 Caesium with other atoms in the Cs 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
A:Cs311

b:11.6
occ:0.10
 CS A:CS311 0.0 11.6 0.1
CS A:CS311 1.5 16.2 0.9
O A:HOH547 2.3 30.9 1.0
O A:ARG267 2.6 19.0 1.0
O A:ALA265 3.5 12.6 1.0
O A:HOH466 3.8 45.3 1.0
C A:ARG267 3.9 18.0 1.0
C A:ALA265 4.1 10.5 1.0
O A:HOH676 4.3 34.3 1.0
O A:ALA264 4.3 11.8 1.0
N A:ARG267 4.3 13.7 1.0
OG A:SER221 4.4 12.6 0.7
CA A:ALA265 4.6 10.8 1.0
CA A:ARG267 4.7 16.3 1.0
O A:HOH525 4.8 25.0 1.0
C A:SER266 4.8 12.3 1.0
N A:ALA268 4.8 20.0 1.0
C A:ALA268 4.9 25.9 1.0
O A:ALA268 4.9 32.3 1.0
CB A:SER221 5.0 9.4 0.3
CA A:ALA268 5.0 22.5 1.0
N A:SER266 5.0 10.5 1.0

Caesium binding site 5 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 5 out of 8 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 Caesium with other atoms in the Cs binding site number 5 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:Cs521

b:18.8
occ:0.50
 O B:HOH1011 2.9 33.1 1.0
O B:SER249 3.0 13.8 1.0
O B:ASP225 3.1 8.8 1.0
O B:HOH732 3.2 19.8 1.0
N B:GLY251 4.0 7.9 1.0
C B:ASP225 4.1 8.1 1.0
O B:HOH914 4.1 33.6 1.0
C B:SER249 4.1 12.9 1.0
CA B:ASP225 4.3 8.4 1.0
O B:HOH1022 4.4 17.5 1.0
O B:HOH820 4.5 27.2 1.0
CB B:ASP225 4.5 9.0 1.0
CA B:GLY251 4.6 8.3 1.0
C B:VAL250 4.8 8.2 1.0
O B:HOH1030 4.8 18.5 1.0
CA B:VAL250 4.9 8.6 1.0
OD1 B:ASP225 4.9 13.1 1.0
N B:VAL250 5.0 10.0 1.0

Caesium binding site 6 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 6 out of 8 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 Caesium with other atoms in the Cs binding site number 6 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:Cs522

b:11.3
occ:0.80
 CS B:CS522 0.0 11.3 0.8
CS B:CS522 1.9 18.7 0.2
O B:GLY232 2.8 15.7 1.0
O B:PHE306 3.0 12.0 1.0
O B:GLY268 3.1 8.7 1.0
O B:SER308 3.3 9.5 1.0
O B:LEU304 3.4 11.2 1.0
C B:GLY232 3.8 9.5 1.0
O B:VAL231 3.9 8.4 1.0
C B:PHE306 4.0 11.3 1.0
CD B:PRO270 4.0 8.4 1.0
C B:GLY268 4.1 8.4 1.0
CA B:GLY232 4.1 8.2 1.0
N B:PHE306 4.3 11.3 1.0
CG B:PRO270 4.4 9.5 1.0
CB B:PHE306 4.4 12.6 1.0
CA B:PHE306 4.5 11.6 1.0
C B:SER308 4.5 8.4 1.0
CD B:PRO257 4.5 7.3 1.0
C B:LEU304 4.5 9.8 1.0
CA B:GLY268 4.6 9.2 1.0
C B:VAL231 4.7 7.1 1.0
CG B:PRO257 4.7 7.5 1.0
N B:SER308 4.8 9.6 1.0
N B:GLY232 4.8 7.2 1.0
OE2 B:GLU256 5.0 8.8 1.0

Caesium binding site 7 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 7 out of 8 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 Caesium with other atoms in the Cs binding site number 7 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:Cs522

b:18.7
occ:0.20
 CS B:CS522 0.0 18.7 0.2
CS B:CS522 1.9 11.3 0.8
O B:GLY232 3.2 15.7 1.0
O B:VAL231 3.3 8.4 1.0
O B:GLY268 3.3 8.7 1.0
O B:SER308 3.4 9.5 1.0
OE2 B:GLU256 3.4 8.8 1.0
CD B:PRO270 3.6 8.4 1.0
CG B:PRO270 3.9 9.5 1.0
CB B:VAL309 4.1 9.5 1.0
C B:VAL231 4.1 7.1 1.0
C B:GLY232 4.1 9.5 1.0
CG1 B:VAL231 4.2 8.6 1.0
CG2 B:VAL309 4.2 9.9 1.0
CD B:GLU256 4.3 8.8 1.0
CG B:GLU256 4.3 8.6 1.0
C B:SER308 4.4 8.4 1.0
C B:GLY268 4.4 8.4 1.0
CA B:GLY232 4.5 8.2 1.0
O B:PHE306 4.6 12.0 1.0
CD B:PRO257 4.6 7.3 1.0
CB B:GLU256 4.6 7.5 1.0
N B:GLY232 4.7 7.2 1.0
CA B:VAL309 4.7 7.8 1.0
CB B:VAL231 4.8 7.7 1.0
N B:PRO270 4.8 8.0 1.0
O B:LEU304 5.0 11.2 1.0
CA B:ALA269 5.0 8.2 1.0

Caesium binding site 8 out of 8 in 7lkl

Go back to Caesium Binding Sites List in 7lkl
Caesium binding site 8 out of 8 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 Caesium with other atoms in the Cs binding site number 8 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:Cs523

b:12.0
occ:1.00
 O B:THR71 3.0 8.9 1.0
O B:THR69 3.0 10.3 1.0
O B:HOH738 3.2 20.1 1.0
O B:HOH959 3.2 47.0 1.0
O B:THR66 3.2 10.6 1.0
OG1 B:THR66 3.2 10.4 1.0
O B:HOH810 3.3 24.6 1.0
O B:HOH654 3.6 33.0 1.0
O B:HOH983 3.8 22.8 1.0
CB B:THR66 3.9 9.7 1.0
C B:THR66 3.9 10.7 1.0
C B:THR69 4.1 9.8 1.0
C B:THR71 4.1 7.6 1.0
OG1 B:THR69 4.3 9.2 1.0
O B:HOH870 4.5 41.6 1.0
N B:ALA67 4.5 10.9 1.0
N B:THR69 4.6 11.5 1.0
CA B:THR66 4.6 9.9 1.0
N B:THR71 4.6 7.9 1.0
CA B:ALA67 4.6 13.4 1.0
O B:HOH731 4.6 9.6 1.0
CA B:THR69 4.8 10.3 1.0
N B:GLY68 4.9 15.1 1.0
N B:ARG70 4.9 8.8 1.0
N B:THR72 4.9 7.3 1.0
C B:ARG70 5.0 8.5 1.0
CA B:ARG70 5.0 9.5 1.0
CA B:THR71 5.0 7.6 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.
Page generated: Tue Jul 30 21:16:06 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy