Sodium in PDB 2wsy: Crystal Structure of Wild-Type Tryptophan Synthase

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase:
4.2.1.20;

The structure of Crystal Structure of Wild-Type Tryptophan Synthase, PDB code: 2wsy was solved by T.R.Schneider, E.Gerhardt, M.Lee, P.-H.Liang, K.S.Anderson, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 3.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	185.100, 61.200, 67.600, 90.00, 94.70, 90.00
R / Rfree (%)	19.7 / 29.9

The binding sites of Sodium atom in the Crystal Structure of Wild-Type Tryptophan Synthase (pdb code 2wsy). 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, PDB code: 2wsy:

Sodium binding site 1 out of 1 in the Crystal Structure of Wild-Type Tryptophan Synthase


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Na2000 b:2.0 occ:1.00 O B:GLY232 2.6 8.7 1.0 O B:PHE306 2.6 10.5 1.0 O B:SER308 2.9 8.1 1.0 C B:GLY232 3.3 8.2 1.0 CA B:GLY232 3.7 7.2 1.0 C B:PHE306 3.8 11.0 1.0 O B:VAL231 3.8 4.0 1.0 O B:GLY268 4.0 18.6 1.0 CD B:PRO270 4.1 16.8 1.0 C B:SER308 4.2 8.5 1.0 CB B:PHE306 4.2 9.6 1.0 CG B:PRO270 4.3 16.5 1.0 CA B:PHE306 4.4 10.5 1.0 N B:PHE306 4.4 10.6 1.0 N B:SER308 4.4 9.2 1.0 N B:GLY233 4.5 9.1 1.0 C B:VAL231 4.5 4.5 1.0 N B:GLY232 4.5 5.5 1.0 CG1 B:VAL231 4.8 2.0 1.0 N B:PRO307 4.9 11.0 1.0 O B:LEU304 4.9 16.9 1.0 CA B:SER308 4.9 9.4 1.0 CD2 B:PHE306 4.9 7.9 1.0 CG B:PHE306 5.0 8.1 1.0 CA B:GLY233 5.0 5.3 1.0 C B:GLY268 5.0 19.0 1.0

T.R.Schneider, E.Gerhardt, M.Lee, P.H.Liang, K.S.Anderson, I.Schlichting. Loop Closure and Intersubunit Communication in Tryptophan Synthase. Biochemistry V. 37 5394 1998.
ISSN: ISSN 0006-2960
PubMed: 9548921
DOI: 10.1021/BI9728957