Sodium in PDB 8ezc: X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine

All present enzymatic activity of X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine:
4.2.1.20;

The structure of X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine, PDB code: 8ezc was solved by V.N.Drago, T.C.Mueser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.84 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	184.549, 58.82, 67.29, 90, 94.81, 90
R / Rfree (%)	19.5 / 20.3

The binding sites of Sodium atom in the X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine (pdb code 8ezc). 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 X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine, PDB code: 8ezc:

Sodium binding site 1 out of 1 in the X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Crystal Structure of Salmonella Typhimurium Tryptophan Synthase Internal Aldimine within 5.0Å range: probe atom residue distance (Å) B Occ B:Na401 b:19.4 occ:1.00 O B:GLY232 2.2 19.6 1.0 O B:HOH529 2.3 25.2 1.0 O B:HOH610 2.3 18.6 1.0 O B:SER308 2.3 14.8 1.0 O B:PHE306 2.5 25.9 1.0 C B:GLY232 3.3 17.4 1.0 C B:SER308 3.5 18.4 1.0 C B:PHE306 3.6 25.4 1.0 CB B:PHE306 3.6 28.4 1.0 CG B:PRO270 3.9 16.9 1.0 CD B:PRO270 3.9 13.2 1.0 CA B:GLY232 3.9 16.6 1.0 O B:GLY268 4.0 18.6 1.0 CD2 B:PHE306 4.0 25.4 1.0 N B:SER308 4.0 19.3 1.0 CA B:PHE306 4.1 27.4 1.0 CG B:PHE306 4.3 26.8 1.0 O B:VAL231 4.3 16.1 1.0 N B:PHE306 4.4 27.9 1.0 CA B:SER308 4.4 17.4 1.0 N B:VAL309 4.4 15.9 1.0 O B:LEU304 4.4 21.7 1.0 N B:GLY233 4.5 15.1 1.0 CA B:VAL309 4.5 13.8 1.0 CB B:VAL309 4.6 15.3 1.0 N B:PRO307 4.6 26.6 1.0 C B:PRO307 4.7 22.1 1.0 OE2 B:GLU256 4.8 15.6 1.0 CA B:GLY233 4.8 13.9 1.0 N B:GLY232 4.9 15.3 1.0 C B:GLY268 4.9 15.7 1.0 CA B:PRO307 4.9 25.0 1.0 C B:VAL231 4.9 14.7 1.0

V.N.Drago, J.M.Devos, M.P.Blakeley, V.T.Forsyth, J.M.Parks, A.Kovalevsky, T.C.Mueser. Microgravity-Assisted Neutron Crystallography Reveals Functional Hydrogen Atoms in the Resting State of Tryptophan Synthase Cell Rep Phys Sci 2024.
ISSN: ESSN 2666-3864
DOI: 10.1016/J.XCRP.2024.101827