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Caesium in PDB 7l47: The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site

Enzymatic activity of The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site

All present enzymatic activity of The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site:
4.2.1.20;

Protein crystallography data

The structure of The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site, PDB code: 7l47 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) 38.94 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 181.979, 59.33, 67.07, 90, 94.34, 90
R / Rfree (%) 18.8 / 21.2

Other elements in 7l47:

The structure of The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site also contains other interesting chemical elements:

Chlorine (Cl) 11 atoms

Caesium Binding Sites:

The binding sites of Caesium atom in the The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site (pdb code 7l47). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 4 binding sites of Caesium where determined in the The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site, PDB code: 7l47:
Jump to Caesium binding site number: 1; 2; 3; 4;

Caesium binding site 1 out of 4 in 7l47

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Caesium binding site 1 out of 4 in the The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site


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 Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cs306

b:35.7
occ:0.45
 O A:ALA167 3.0 26.1 1.0
O A:HOH616 3.0 54.5 1.0
O A:GLY170 3.1 23.2 1.0
O A:HIS204 3.5 26.2 1.0
O A:HOH450 3.5 37.4 1.0
N A:ALA206 4.0 21.2 1.0
O A:HOH565 4.1 60.7 1.0
NH2 A:ARG171 4.2 30.4 1.0
O A:SER168 4.3 26.9 1.0
C A:ALA167 4.3 24.7 1.0
CD A:ARG171 4.3 25.9 1.0
C A:GLY170 4.3 21.4 1.0
C A:ALA205 4.3 21.6 1.0
CA A:ALA205 4.4 21.5 1.0
C A:HIS204 4.5 26.1 1.0
C A:SER168 4.7 26.3 1.0
NE A:ARG171 4.8 28.9 1.0
CZ A:ARG171 4.8 30.4 1.0
CA A:ALA206 4.8 20.2 1.0
CB A:ALA206 4.9 19.9 1.0
CA A:SER168 5.0 26.0 1.0
N A:ALA205 5.0 24.0 1.0

Caesium binding site 2 out of 4 in 7l47

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Caesium binding site 2 out of 4 in the The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site


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 Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs419

b:18.7
occ:0.68
 O B:THR71 3.0 15.6 1.0
O B:THR69 3.2 19.3 1.0
O B:HOH645 3.3 28.8 1.0
OG1 B:THR66 3.3 17.1 1.0
O B:HOH675 3.4 42.2 1.0
O B:THR66 3.4 18.4 1.0
O B:HOH853 3.7 35.8 1.0
CB B:THR66 3.9 17.1 1.0
C B:THR66 4.0 18.7 1.0
C B:THR71 4.1 15.2 1.0
C B:THR69 4.1 18.3 1.0
OG1 B:THR69 4.3 16.7 1.0
N B:THR71 4.5 14.8 1.0
CA B:THR66 4.6 17.9 1.0
N B:ALA67 4.6 18.9 1.0
O B:HOH607 4.6 14.6 1.0
N B:THR69 4.6 19.7 1.0
CA B:ALA67 4.7 20.9 1.0
N B:GLY68 4.9 22.8 1.0
C B:ARG70 4.9 16.7 0.2
CA B:ARG70 4.9 17.3 0.2
CA B:THR69 4.9 18.6 1.0
C B:ARG70 4.9 17.1 0.8
N B:ARG70 4.9 17.7 0.2
N B:THR72 4.9 14.9 1.0
N B:ARG70 4.9 18.2 0.8
CA B:ARG70 5.0 18.3 0.8
CA B:THR71 5.0 14.6 1.0
O B:HOH790 5.0 51.9 1.0

Caesium binding site 3 out of 4 in 7l47

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Caesium binding site 3 out of 4 in the The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site


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 Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs420

b:15.3
occ:0.76
 CS B:CS420 0.0 15.3 0.8
CS B:CS420 1.4 27.4 0.2
O B:GLY232 3.0 19.6 1.0
O B:GLY268 3.1 14.7 1.0
O B:PHE306 3.1 20.0 1.0
O B:SER308 3.3 16.9 1.0
O B:LEU304 3.4 17.4 1.0
O B:VAL231 3.7 15.9 1.0
C B:GLY232 3.8 16.2 1.0
CA B:GLY232 4.0 15.9 1.0
CD B:PRO270 4.0 14.4 1.0
C B:PHE306 4.1 20.4 1.0
C B:GLY268 4.1 14.0 1.0
N B:PHE306 4.2 21.5 1.0
CD B:PRO257 4.4 14.0 1.0
CB B:PHE306 4.4 23.0 1.0
CG B:PRO270 4.4 14.6 1.0
C B:LEU304 4.5 17.1 1.0
C B:SER308 4.5 17.8 1.0
CA B:PHE306 4.5 21.4 1.0
C B:VAL231 4.5 15.3 1.0
CG B:PRO257 4.6 14.0 1.0
CA B:GLY268 4.7 14.7 1.0
N B:GLY232 4.7 15.4 1.0
N B:SER308 4.9 18.4 1.0
OE1 B:GLU256 4.9 16.7 1.0

Caesium binding site 4 out of 4 in 7l47

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Caesium binding site 4 out of 4 in the The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site


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 Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs420

b:27.4
occ:0.24
 CS B:CS420 0.0 27.4 0.2
CS B:CS420 1.4 15.3 0.8
O B:GLY232 2.7 19.6 1.0
O B:SER308 3.2 16.9 1.0
O B:VAL231 3.2 15.9 1.0
O B:GLY268 3.5 14.7 1.0
C B:GLY232 3.7 16.2 1.0
CD B:PRO270 3.8 14.4 1.0
OE1 B:GLU256 3.9 16.7 1.0
C B:VAL231 4.0 15.3 1.0
CG B:PRO270 4.1 14.6 1.0
CA B:GLY232 4.1 15.9 1.0
CB B:VAL309 4.1 18.0 1.0
C B:SER308 4.2 17.8 1.0
CG1 B:VAL231 4.2 14.3 1.0
O B:PHE306 4.3 20.0 1.0
N B:GLY232 4.4 15.4 1.0
CG2 B:VAL309 4.5 19.0 1.0
C B:GLY268 4.6 14.0 1.0
CA B:VAL309 4.6 17.4 1.0
O B:LEU304 4.6 17.4 1.0
CD B:PRO257 4.6 14.0 1.0
N B:VAL309 4.8 17.0 1.0
CB B:VAL231 4.8 14.6 1.0
CD B:GLU256 4.9 16.3 1.0
CG B:GLU256 4.9 15.3 1.0
N B:GLY233 4.9 15.4 1.0

Reference:

E.Hilario, M.F.Dunn, L.J.Mueller. The Internal Aldimine Form of the Beta-K167T Mutant Tryptophan Synthase From Salmonella at 1.55 Angstrom Resolution with Cesium Ion at the Metal Coordination Site. To Be Published.
Page generated: Tue Jul 30 21:15:14 2024

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