Potassium in PDB 1ttq: Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature

All present enzymatic activity of Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature:
4.2.1.20;

The structure of Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature, PDB code: 1ttq was solved by S.Rhee, K.Parris, S.Ahmed, E.W.Miles, D.R.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	185.000, 61.300, 67.700, 90.00, 94.70, 90.00
R / Rfree (%)	21.7 / 28.5

The binding sites of Potassium atom in the Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature (pdb code 1ttq). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature, PDB code: 1ttq:

Potassium binding site 1 out of 1 in the Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Tryptophan Synthase (E.C.4.2.1.20) in the Presence of Potassium at Room Temperature within 5.0Å range: probe atom residue distance (Å) B Occ B:K400 b:32.1 occ:1.00 O B:GLY232 2.2 17.0 1.0 O B:PHE306 2.7 31.8 1.0 O B:HOH448 2.7 15.6 1.0 O B:SER308 3.0 14.3 1.0 C B:GLY232 3.3 18.4 1.0 C B:PHE306 3.8 31.0 1.0 CA B:GLY232 3.9 15.8 1.0 O B:GLY268 3.9 14.2 1.0 CD B:PRO270 4.0 26.7 1.0 CG B:PRO270 4.0 24.4 1.0 C B:SER308 4.1 14.1 1.0 CG1 B:VAL309 4.1 21.8 1.0 O B:VAL231 4.2 11.6 1.0 N B:SER308 4.2 16.7 1.0 OG B:SER297 4.3 49.6 1.0 CB B:PHE306 4.3 23.9 1.0 N B:GLY233 4.4 18.1 1.0 O B:LEU304 4.4 39.1 1.0 CA B:PHE306 4.5 28.8 1.0 N B:PHE306 4.6 32.1 1.0 CA B:SER308 4.8 15.0 1.0 CD2 B:PHE306 4.8 21.2 1.0 C B:VAL231 4.8 15.1 1.0 N B:PRO307 4.8 30.2 1.0 N B:GLY232 4.8 15.3 1.0 CA B:GLY233 4.8 11.7 1.0 C B:GLY268 4.9 17.7 1.0 C B:PRO307 4.9 20.6 1.0 N B:VAL309 5.0 12.9 1.0 CG B:PHE306 5.0 24.0 1.0 CA B:PRO307 5.0 27.4 1.0

S.Rhee, K.D.Parris, S.A.Ahmed, E.W.Miles, D.R.Davies. Exchange of K+ or Cs+ For Na+ Induces Local and Long-Range Changes in the Three-Dimensional Structure of the Tryptophan Synthase ALPHA2BETA2 Complex. Biochemistry V. 35 4211 1996.
ISSN: ISSN 0006-2960
PubMed: 8672457
DOI: 10.1021/BI952506D