Sodium in PDB 2j9y: Tryptophan Synthase Q114N Mutant in Complex with Compound II

All present enzymatic activity of Tryptophan Synthase Q114N Mutant in Complex with Compound II:
4.2.1.20;

The structure of Tryptophan Synthase Q114N Mutant in Complex with Compound II, PDB code: 2j9y 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)	19.45 / 1.8
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	182.740, 60.700, 67.410, 90.00, 94.83, 90.00
R / Rfree (%)	22.8 / 26.3

The binding sites of Sodium atom in the Tryptophan Synthase Q114N Mutant in Complex with Compound II (pdb code 2j9y). 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 Q114N Mutant in Complex with Compound II, PDB code: 2j9y:

Sodium binding site 1 out of 1 in the Tryptophan Synthase Q114N Mutant in Complex with Compound II


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Tryptophan Synthase Q114N Mutant in Complex with Compound II within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1397 b:25.1 occ:1.00 O B:SER308 2.3 18.6 1.0 O B:HOH2264 2.3 27.6 1.0 O B:HOH2299 2.3 31.0 1.0 O B:GLY232 2.3 21.1 1.0 O B:PHE306 3.0 28.6 1.0 C B:GLY232 3.4 19.1 1.0 C B:SER308 3.5 20.1 1.0 O B:GLY268 3.9 15.6 1.0 CA B:GLY232 3.9 16.4 1.0 CB B:PHE306 3.9 28.6 1.0 C B:PHE306 3.9 27.0 1.0 CD B:PRO270 4.0 16.3 1.0 CD2 B:PHE306 4.0 31.7 1.0 CG B:PRO270 4.0 16.1 1.0 O B:VAL231 4.1 14.8 1.0 N B:SER308 4.2 20.3 1.0 CB B:VAL309 4.4 18.0 1.0 CA B:VAL309 4.4 16.8 1.0 CA B:PHE306 4.4 27.7 1.0 N B:VAL309 4.4 18.5 1.0 CG B:PHE306 4.4 31.4 1.0 CA B:SER308 4.5 18.8 1.0 O B:LEU304 4.5 19.2 1.0 N B:GLY233 4.5 16.7 1.0 N B:PHE306 4.7 26.7 1.0 OE2 B:GLU256 4.7 20.1 1.0 N B:GLY232 4.7 17.0 1.0 C B:VAL231 4.8 15.7 1.0 C B:GLY268 4.8 15.4 1.0 CG2 B:VAL309 4.9 17.3 1.0 N B:PRO307 4.9 25.3 1.0 C B:PRO307 4.9 22.9 1.0 CA B:GLY233 5.0 17.5 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