Potassium in PDB 8egz: Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate

All present enzymatic activity of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate:
4.2.1.20;

The structure of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate, PDB code: 8egz was solved by N.J.Porter, P.J.Almhjell, F.H.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.13 / 1.90
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	164.566, 164.566, 84.254, 90, 90, 90
R / Rfree (%)	17 / 19.2

The binding sites of Potassium atom in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate (pdb code 8egz). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate, PDB code: 8egz:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate within 5.0Å range: probe atom residue distance (Å) B Occ A:K406 b:32.3 occ:1.00 O A:HOH506 2.5 40.8 1.0 O A:TYR301 2.6 29.0 1.0 O A:HOH516 2.7 31.6 1.0 O A:GLY303 2.7 24.5 1.0 O A:ALA263 2.8 26.0 1.0 OG A:SER265 2.8 29.1 1.0 O A:SER228 3.7 32.6 1.0 O A:HOH570 3.7 29.1 1.0 C A:GLY303 3.7 25.0 1.0 C A:TYR301 3.7 29.8 1.0 C A:ALA263 3.9 26.9 1.0 CB A:SER265 3.9 25.2 1.0 N A:GLY303 4.0 28.1 1.0 C A:SER228 4.0 27.6 1.0 CA A:SER228 4.1 36.1 1.0 N A:SER265 4.2 26.9 1.0 C A:PRO302 4.2 26.7 1.0 CB A:ALA263 4.4 23.4 1.0 CA A:GLY303 4.4 29.8 1.0 O A:LEU299 4.5 26.7 1.0 CA A:PRO302 4.5 24.0 1.0 CB A:TYR301 4.6 25.4 1.0 N A:PRO302 4.6 27.0 1.0 CA A:ALA263 4.6 24.4 1.0 CD2 A:TYR301 4.6 30.2 1.0 CA A:TYR301 4.6 28.3 1.0 OG A:SER228 4.6 53.3 1.0 CA A:SER265 4.7 25.5 1.0 N A:VAL304 4.7 25.4 1.0 O A:PRO302 4.7 26.1 1.0 CB A:SER228 4.8 41.1 1.0 N A:TYR301 4.8 27.4 1.0 OE2 A:GLU251 4.8 31.3 1.0 CB A:VAL304 4.9 25.2 1.0 N A:ALA264 4.9 23.9 1.0 CA A:VAL304 4.9 26.2 1.0 N A:GLY229 5.0 26.6 1.0

Potassium binding site 2 out of 2 in the Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Engineered Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb with Ser Bound As the Amino-Acrylate Intermediate within 5.0Å range: probe atom residue distance (Å) B Occ B:K404 b:36.0 occ:1.00 O B:HOH514 2.6 32.3 1.0 O B:GLY303 2.7 28.7 1.0 O B:TYR301 2.7 28.8 1.0 O B:ALA263 2.8 26.4 1.0 OG B:SER265 2.8 32.4 1.0 OG B:SER228 3.0 44.6 1.0 O B:HOH543 3.7 33.9 1.0 O B:SER228 3.8 31.9 1.0 C B:GLY303 3.8 29.2 1.0 CB B:SER265 3.8 33.9 1.0 C B:TYR301 3.9 29.5 1.0 C B:ALA263 3.9 32.6 1.0 CA B:SER228 3.9 40.0 1.0 C B:SER228 4.0 30.6 1.0 N B:SER265 4.1 31.6 1.0 CB B:ALA263 4.1 31.4 1.0 CB B:SER228 4.1 38.9 1.0 N B:GLY303 4.2 27.6 1.0 C B:PRO302 4.3 30.7 1.0 CA B:ALA263 4.5 27.1 1.0 O B:LEU299 4.5 32.8 1.0 CA B:GLY303 4.5 25.5 1.0 CA B:SER265 4.6 32.0 1.0 CA B:PRO302 4.6 28.7 1.0 N B:PRO302 4.7 29.9 1.0 CB B:TYR301 4.7 25.2 1.0 CD2 B:TYR301 4.7 34.6 1.0 OE2 B:GLU251 4.7 38.4 1.0 CA B:TYR301 4.7 29.3 1.0 N B:VAL304 4.7 32.4 1.0 O B:PRO302 4.8 31.2 1.0 CB B:VAL304 4.8 30.1 1.0 N B:TYR301 4.9 30.6 1.0 N B:ALA264 4.9 30.8 1.0 N B:GLY229 4.9 28.8 1.0 CA B:VAL304 4.9 27.6 1.0

N.J.Porter, P.J.Almhjell, F.H.Arnold. Noncanonical L-Tyrosine Synthesis By Evolved Tryptophan Synthases To Be Published.