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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

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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

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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

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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

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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

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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

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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

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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

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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

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