Sodium in PDB 1kfj: Crystal Structure of Wild-Type Tryptophan Synthase Complexed with L-Serine

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with L-Serine:
4.2.1.20;

The structure of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with L-Serine, PDB code: 1kfj was solved by V.Kulik, M.Weyand, R.Seidel, 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)	20.00 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	183.230, 59.679, 67.462, 90.00, 94.65, 90.00
R / Rfree (%)	17.4 / 21.1

The binding sites of Sodium atom in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with L-Serine (pdb code 1kfj). 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 Wild-Type Tryptophan Synthase Complexed with L-Serine, PDB code: 1kfj:

Sodium binding site 1 out of 1 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with L-Serine


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 Wild-Type Tryptophan Synthase Complexed with L-Serine within 5.0Å range: probe atom residue distance (Å) B Occ B:Na399 b:26.8 occ:1.00 O B:GLY232 2.3 27.4 1.0 O B:SER308 2.3 23.2 1.0 O B:HOH448 2.3 28.1 1.0 O B:PHE306 2.5 32.5 1.0 O B:HOH533 2.5 29.6 1.0 C B:GLY232 3.4 26.9 1.0 C B:SER308 3.5 22.4 1.0 C B:PHE306 3.6 31.6 1.0 N B:SER308 3.9 25.4 1.0 CG B:PRO270 3.9 19.3 1.0 CA B:GLY232 4.0 23.0 1.0 CD B:PRO270 4.0 19.2 1.0 O B:GLY268 4.2 27.0 1.0 CB B:PHE306 4.3 34.2 1.0 CD2 B:PHE306 4.3 32.1 1.0 CA B:SER308 4.4 23.2 1.0 CA B:PHE306 4.4 31.4 1.0 O B:VAL231 4.5 23.4 1.0 N B:GLY233 4.5 22.8 1.0 OG B:SER297 4.5 37.2 1.0 N B:VAL309 4.5 23.6 1.0 C B:PRO307 4.5 27.9 1.0 CA B:VAL309 4.6 21.2 1.0 N B:PRO307 4.6 33.0 1.0 N B:PHE306 4.6 34.4 1.0 CA B:PRO307 4.7 27.1 1.0 O B:LEU304 4.7 30.5 1.0 CB B:VAL309 4.7 19.7 1.0 OE2 B:GLU256 4.7 27.8 1.0 CA B:GLY233 4.7 22.2 1.0 CG B:PHE306 4.8 30.2 1.0 N B:GLY232 4.9 23.5 1.0

V.Kulik, M.Weyand, R.Seidel, 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