Sodium in PDB 2j9z: Tryptophan Synthase T110 Mutant Complex

All present enzymatic activity of Tryptophan Synthase T110 Mutant Complex:
4.2.1.20;

The structure of Tryptophan Synthase T110 Mutant Complex, PDB code: 2j9z was solved by L.Blumenstein, T.Domratcheva, D.Niks, H.Ngo, R.Seidel, M.F.Dunn, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.85 / 1.8
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	182.800, 59.900, 67.600, 90.00, 94.40, 90.00
R / Rfree (%)	18.7 / 21.8

The binding sites of Sodium atom in the Tryptophan Synthase T110 Mutant Complex (pdb code 2j9z). 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 Tryptophan Synthase T110 Mutant Complex, PDB code: 2j9z:

Sodium binding site 1 out of 1 in the Tryptophan Synthase T110 Mutant Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Tryptophan Synthase T110 Mutant Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1396 b:11.2 occ:1.00 O B:GLY232 2.3 11.4 1.0 O B:HOH2248 2.3 11.7 1.0 O B:SER308 2.3 8.6 1.0 O B:PHE306 2.4 20.7 1.0 O B:HOH2281 2.4 16.4 1.0 C B:GLY232 3.4 9.0 1.0 C B:PHE306 3.5 19.4 1.0 C B:SER308 3.6 9.4 1.0 CG B:PRO270 3.8 9.8 1.0 CB B:PHE306 3.8 20.4 1.0 CA B:GLY232 4.0 7.5 1.0 CD B:PRO270 4.0 10.7 1.0 CD2 B:PHE306 4.0 16.4 1.0 N B:SER308 4.1 12.2 1.0 CA B:PHE306 4.1 20.9 1.0 O B:GLY268 4.1 13.0 1.0 N B:PHE306 4.3 23.2 1.0 CG B:PHE306 4.4 19.1 1.0 O B:VAL231 4.4 8.7 1.0 CA B:SER308 4.4 9.9 1.0 O B:LEU304 4.5 15.9 1.0 N B:VAL309 4.5 8.7 1.0 N B:GLY233 4.5 6.6 1.0 CA B:VAL309 4.5 8.2 1.0 N B:PRO307 4.6 18.5 1.0 C B:PRO307 4.6 14.3 1.0 CB B:VAL309 4.6 6.8 1.0 OE2 B:GLU256 4.8 10.6 1.0 N B:GLY232 4.9 7.7 1.0 CA B:GLY233 4.9 6.4 1.0 OG B:SER297 4.9 31.9 1.0 CA B:PRO307 4.9 16.0 1.0 C B:VAL231 5.0 7.3 1.0

L.Blumenstein, T.Domratcheva, D.Niks, H.Ngo, R.Seidel, M.F.Dunn, I.Schlichting. BETAQ114N and BETAT110V Mutations Reveal A Critically Important Role of the Substrate Alpha- Carboxylate Site in the Reaction Specificity of Tryptophan Synthase. Biochemistry V. 46 14100 2007.
ISSN: ISSN 0006-2960
PubMed: 18004874
DOI: 10.1021/BI7008568