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Sodium in PDB 1kfc: Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate

Enzymatic activity of Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate

All present enzymatic activity of Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate:
4.2.1.20;

Protein crystallography data

The structure of Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate, PDB code: 1kfc was solved by V.Kulik, M.Weyand, R.Siedel, D.Niks, D.Arac, M.F.Dunn, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.99 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 181.419, 60.343, 66.991, 90.00, 94.56, 90.00
R / Rfree (%) 19.5 / 22.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate (pdb code 1kfc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate, PDB code: 1kfc:

Sodium binding site 1 out of 1 in 1kfc

Go back to Sodium Binding Sites List in 1kfc
Sodium binding site 1 out of 1 in the Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of ALPHAT183V Mutant of Tryptophan Synthase From Salmonella Typhimurium with Indole Propanol Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na676

b:14.2
occ:1.00
 O B:GLY232 2.2 13.1 1.0
O B:SER308 2.3 14.0 1.0
O B:PHE306 2.4 19.5 1.0
O B:HOH732 2.4 16.4 1.0
O B:HOH699 2.4 13.6 1.0
C B:GLY232 3.4 11.8 1.0
C B:SER308 3.5 13.9 1.0
C B:PHE306 3.5 18.0 1.0
CG B:PRO270 3.7 12.6 1.0
CD B:PRO270 3.9 10.3 1.0
N B:SER308 3.9 15.9 1.0
O B:GLY268 4.0 13.0 1.0
CA B:GLY232 4.1 10.8 1.0
OG B:SER297 4.3 26.6 1.0
CB B:PHE306 4.3 18.7 1.0
CA B:SER308 4.3 15.7 1.0
CA B:PHE306 4.3 17.6 1.0
CD2 B:PHE306 4.4 16.6 1.0
O B:VAL231 4.4 11.7 1.0
C B:PRO307 4.5 17.4 1.0
N B:VAL309 4.5 12.4 1.0
N B:GLY233 4.5 12.0 1.0
N B:PRO307 4.5 18.3 1.0
N B:PHE306 4.6 19.2 1.0
CA B:VAL309 4.6 11.5 1.0
CB B:VAL309 4.7 12.1 1.0
CA B:PRO307 4.7 17.7 1.0
O B:LEU304 4.7 16.9 1.0
OE2 B:GLU256 4.8 12.5 1.0
CA B:GLY233 4.8 9.9 1.0
CG B:PHE306 4.8 16.9 1.0
N B:GLY232 4.9 10.9 1.0
C B:VAL231 5.0 10.9 1.0
C B:GLY268 5.0 13.4 1.0

Reference:

V.Kulik, M.Weyand, R.Siedel, D.Niks, D.Arac, M.F.Dunn, I.Schlichting. On the Role of ALPHATHR183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase J.Mol.Biol. V. 324 677 2002.
ISSN: ISSN 0022-2836
PubMed: 12460570
DOI: 10.1016/S0022-2836(02)01109-9
Page generated: Sun Aug 17 06:06:10 2025

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