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

Caesium in PDB 7lut: The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution

Enzymatic activity of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution

All present enzymatic activity of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution:
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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution, PDB code: 7lut 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) 32.28 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.412, 61.086, 67.063, 90, 94.86, 90
R / Rfree (%) 18.7 / 21.7

Other elements in 7lut:

The structure of The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution also contains other interesting chemical elements:

Chlorine (Cl) 5 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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution (pdb code 7lut). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 7 binding sites of Caesium where determined in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution, PDB code: 7lut:
Jump to Caesium binding site number: 1; 2; 3; 4; 5; 6; 7;

Caesium binding site 1 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 1 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cs304

b:22.6
occ:0.60
 O A:HOH573 2.8 37.1 1.0
O A:ALA167 3.0 16.2 1.0
O A:GLY170 3.1 16.2 1.0
O A:HIS204 3.4 19.2 1.0
O A:HOH534 3.6 15.2 0.4
O A:HOH461 3.9 37.0 1.0
N A:ALA206 4.0 15.3 1.0
NH1 A:ARG171 4.1 19.8 1.0
C A:ALA167 4.2 15.9 1.0
C A:GLY170 4.2 13.9 1.0
O A:HOH437 4.2 12.2 0.3
O A:SER168 4.2 17.6 1.0
CD A:ARG171 4.3 16.9 1.0
C A:ALA205 4.4 15.9 1.0
CA A:ALA205 4.4 16.0 1.0
O A:HOH481 4.5 38.2 1.0
C A:HIS204 4.5 19.4 1.0
C A:SER168 4.7 17.1 1.0
CZ A:ARG171 4.8 19.4 1.0
CA A:ALA206 4.8 14.5 1.0
O A:HOH619 4.9 42.9 1.0
NE A:ARG171 4.9 18.9 1.0
CA A:SER168 4.9 17.2 1.0
N A:GLY170 4.9 14.5 1.0
CB A:ALA206 5.0 14.2 1.0
N A:ALA205 5.0 18.0 1.0
N A:SER168 5.0 16.4 1.0

Caesium binding site 2 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 2 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs408

b:14.7
occ:0.92
 O B:THR71 3.0 11.3 1.0
O B:HOH638 3.1 21.1 1.0
O B:THR69 3.1 14.1 1.0
OG1 B:THR66 3.2 13.6 1.0
O B:THR66 3.2 14.2 1.0
O B:HOH556 3.4 24.5 1.0
O B:HOH844 3.7 25.0 1.0
CB B:THR66 3.8 13.0 1.0
C B:THR66 3.9 14.1 1.0
C B:THR69 4.1 13.5 1.0
C B:THR71 4.1 10.8 1.0
OG1 B:THR69 4.2 12.6 1.0
N B:THR69 4.5 15.2 1.0
N B:THR71 4.5 11.0 1.0
CA B:THR66 4.5 13.6 1.0
N B:ALA67 4.6 14.6 1.0
CA B:ALA67 4.6 15.8 1.0
O B:HOH683 4.6 11.7 1.0
N B:GLY68 4.8 17.5 1.0
CA B:THR69 4.9 14.0 1.0
N B:ARG70 4.9 13.5 1.0
C B:ARG70 4.9 12.3 1.0
CA B:ARG70 4.9 13.2 1.0
CA B:THR71 5.0 11.1 1.0
N B:THR72 5.0 10.8 1.0
C B:ALA67 5.0 16.7 1.0

Caesium binding site 3 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 3 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs409

b:13.2
occ:0.83
 CS B:CS409 0.0 13.2 0.8
CS B:CS409 2.5 26.9 0.2
O B:GLY232 2.9 13.0 1.0
O B:PHE306 2.9 12.8 1.0
O B:GLY268 3.0 9.9 1.0
O B:LEU304 3.3 11.3 1.0
O B:SER308 3.3 11.6 1.0
C B:GLY232 3.8 10.8 1.0
O B:VAL231 3.9 10.2 1.0
C B:PHE306 4.0 13.4 1.0
CA B:GLY232 4.0 10.5 1.0
C B:GLY268 4.0 10.1 1.0
CD B:PRO270 4.1 11.1 1.0
N B:PHE306 4.2 12.8 1.0
CB B:PHE306 4.3 13.9 1.0
C B:LEU304 4.4 11.2 1.0
CA B:PHE306 4.5 13.5 1.0
CD B:PRO257 4.5 8.8 1.0
CG B:PRO270 4.5 11.6 1.0
CA B:GLY268 4.5 10.5 1.0
C B:SER308 4.5 11.8 1.0
CG B:PRO257 4.6 9.0 1.0
C B:VAL231 4.7 9.7 1.0
N B:SER308 4.9 12.7 1.0
N B:GLY232 4.9 10.0 1.0
OE2 B:GLU256 5.0 9.7 1.0

Caesium binding site 4 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 4 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs409

b:26.9
occ:0.17
 CS B:CS409 0.0 26.9 0.2
CS B:CS409 2.5 13.2 0.8
OE2 B:GLU256 2.9 9.7 1.0
O B:VAL231 3.2 10.2 1.0
O B:GLY268 3.4 9.9 1.0
O B:GLY232 3.6 13.0 1.0
CD B:PRO270 3.7 11.1 1.0
CG1 B:VAL231 3.8 9.3 1.0
CD B:GLU256 3.8 9.7 1.0
O B:SER308 3.8 11.6 1.0
CG B:GLU256 3.8 9.4 1.0
CB B:VAL309 3.9 11.0 1.0
CG2 B:VAL309 4.0 10.9 1.0
CG B:PRO270 4.0 11.6 1.0
C B:VAL231 4.1 9.7 1.0
CB B:GLU256 4.3 8.9 1.0
CB B:VAL231 4.4 9.1 1.0
C B:GLY232 4.4 10.8 1.0
C B:GLY268 4.5 10.1 1.0
CD B:PRO257 4.6 8.8 1.0
CA B:GLY232 4.6 10.5 1.0
N B:PRO270 4.7 10.8 1.0
C B:SER308 4.7 11.8 1.0
CA B:VAL309 4.8 10.8 1.0
CA B:GLU256 4.8 8.6 1.0
N B:GLY232 4.8 10.0 1.0
CA B:ALA269 4.8 10.5 1.0
CA B:VAL231 4.9 9.1 1.0
CG1 B:VAL309 5.0 11.1 1.0

Caesium binding site 5 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 5 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs413

b:40.8
occ:0.51
 O B:HOH833 2.5 19.5 0.4
O B:HOH833 2.8 15.4 0.6
O B:HOH687 3.0 21.6 1.0
O B:HOH573 3.0 34.1 1.0
O B:SER297 3.0 15.9 1.0
OD1 B:ASP305 3.2 17.0 1.0
O B:HOH804 3.6 31.1 1.0
OD2 B:ASP305 3.6 17.7 1.0
CG B:ASP305 3.7 16.1 1.0
O B:HOH675 3.9 54.2 1.0
C B:SER297 3.9 14.8 1.0
OG B:SER297 4.0 16.2 1.0
N B:SER297 4.1 16.7 1.0
CG2 B:THR165 4.2 23.1 1.0
OE2 B:GLU296 4.2 36.0 1.0
OG1 B:THR165 4.2 24.8 1.0
CA B:SER297 4.5 15.5 1.0
O B:HOH707 4.5 22.5 1.0
CD B:GLU296 4.6 32.1 1.0
CB B:THR165 4.8 23.2 1.0
CB B:GLU296 4.8 22.2 1.0
C B:GLU296 4.8 18.1 1.0
CA B:GLU296 4.8 20.1 1.0
OE1 B:GLU296 4.9 31.1 1.0
CB B:SER297 4.9 15.6 1.0
N B:TYR298 5.0 13.6 1.0
O B:ASP305 5.0 13.2 1.0

Caesium binding site 6 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 6 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs414

b:15.4
occ:0.34
 O B:PRO56 3.1 9.2 1.0
O B:GLY54 3.2 11.6 1.0
C2 B:DMS402 3.5 22.6 1.0
O B:HOH726 3.7 20.9 1.0
O B:HOH691 4.0 15.5 1.0
O B:DMS402 4.0 23.8 1.0
C B:PRO56 4.3 9.2 1.0
C B:GLY54 4.4 10.9 1.0
S B:DMS402 4.4 25.2 1.0
N B:PRO56 4.6 9.7 1.0
C B:ARG55 4.7 9.6 1.0
C1 B:DMS402 4.8 22.6 1.0
CD B:PRO56 4.8 10.0 1.0
O B:ARG55 4.9 10.0 1.0

Caesium binding site 7 out of 7 in 7lut

Go back to Caesium Binding Sites List in 7lut
Caesium binding site 7 out of 7 in the The Internal Aldimine Form of the Wild-Type Salmonella Typhimurium Tryptophan Synthase in Complex with Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution


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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta- Site at 1.60 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs415

b:21.9
occ:0.50
 O B:LYS99 3.0 15.3 1.0
O B:HOH821 3.0 31.0 1.0
C B:LYS99 3.9 14.6 1.0
CA B:LYS99 4.6 14.5 1.0
CB B:LYS99 4.7 16.4 1.0
CA B:GLY102 4.8 17.2 1.0
N B:ARG100 4.8 15.0 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 Cesium Ion at the Metal Coordination Site and the Product L-Tryptophan at the Enzyme Beta-Site at 1.60 Angstrom Resolution. To Be Published.
Page generated: Tue Jul 30 21:17:04 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