Potassium in PDB 1beu: Trp Synthase (D60N-Ipp-Ser) with K+

All present enzymatic activity of Trp Synthase (D60N-Ipp-Ser) with K+:
4.2.1.20;

The structure of Trp Synthase (D60N-Ipp-Ser) with K+, PDB code: 1beu was solved by S.Rhee, A.Mozzarelli, 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 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	182.300, 59.700, 67.400, 90.00, 94.60, 90.00
R / Rfree (%)	21.9 / 27.8

The binding sites of Potassium atom in the Trp Synthase (D60N-Ipp-Ser) with K+ (pdb code 1beu). 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 Trp Synthase (D60N-Ipp-Ser) with K+, PDB code: 1beu:

Potassium binding site 1 out of 1 in the Trp Synthase (D60N-Ipp-Ser) with K+


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Trp Synthase (D60N-Ipp-Ser) with K+ within 5.0Å range: probe atom residue distance (Å) B Occ B:K400 b:31.2 occ:1.00 O B:PHE306 2.5 32.2 1.0 O B:GLY232 2.6 17.0 1.0 O B:HOH454 2.6 23.3 1.0 O B:SER308 2.8 19.5 1.0 C B:GLY232 3.6 15.0 1.0 O B:GLY268 3.6 14.3 1.0 C B:PHE306 3.7 28.5 1.0 CD B:PRO270 3.9 16.0 1.0 CG1 B:VAL309 3.9 21.9 1.0 C B:SER308 3.9 16.3 1.0 CG B:PRO270 3.9 13.2 1.0 CA B:GLY232 4.0 12.6 1.0 CB B:PHE306 4.1 28.3 1.0 O B:VAL231 4.2 12.4 1.0 CA B:PHE306 4.3 28.9 1.0 N B:SER308 4.3 17.6 1.0 N B:PHE306 4.4 31.9 1.0 OG B:SER297 4.4 38.5 1.0 CD2 B:PHE306 4.5 27.9 1.0 O B:LEU304 4.5 27.2 1.0 C B:GLY268 4.7 10.9 1.0 CG B:PHE306 4.7 29.0 1.0 N B:GLY233 4.7 15.3 1.0 CA B:SER308 4.7 16.7 1.0 N B:PRO307 4.7 29.0 1.0 C B:PRO307 4.8 21.1 1.0 N B:VAL309 4.9 13.9 1.0 OE2 B:GLU256 4.9 18.4 1.0 C B:VAL231 4.9 13.1 1.0 N B:GLY232 4.9 13.6 1.0 O B:HOH457 4.9 18.4 1.0 CA B:VAL309 5.0 11.5 1.0 CA B:PRO307 5.0 24.8 1.0

S.Rhee, E.W.Miles, A.Mozzarelli, D.R.Davies. Cryocrystallography and Microspectrophotometry of A Mutant (Alpha D60N) Tryptophan Synthase Alpha 2 Beta 2 Complex Reveals Allosteric Roles of Alpha ASP60. Biochemistry V. 37 10653 1998.
ISSN: ISSN 0006-2960
PubMed: 9692955
DOI: 10.1021/BI980779D