Potassium in PDB 8vhh: Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb

All present enzymatic activity of Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb:
4.2.1.20;

The structure of Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb, PDB code: 8vhh was solved by N.J.Porter, K.E.Johnston, 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)	45.99 / 2.15
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	165.698, 165.698, 83.061, 90, 90, 90
R / Rfree (%)	21.4 / 23.7

The binding sites of Potassium atom in the Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb (pdb code 8vhh). 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 Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb, PDB code: 8vhh:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:35.8 occ:1.00 O A:HOH503 2.5 38.6 1.0 OG A:SER265 2.7 36.1 1.0 O A:TYR301 2.7 35.6 1.0 O A:GLY303 2.7 34.1 1.0 O A:ALA263 2.8 30.1 1.0 OG A:SER228 3.3 48.0 1.0 CB A:SER265 3.6 28.1 1.0 O A:SER228 3.6 44.9 1.0 C A:GLY303 3.7 34.0 1.0 C A:TYR301 3.8 41.6 1.0 O A:HOH540 3.8 34.1 1.0 C A:ALA263 3.9 29.3 1.0 CA A:SER228 3.9 40.1 1.0 C A:SER228 4.0 32.4 1.0 N A:SER265 4.0 30.1 1.0 N A:GLY303 4.1 30.4 1.0 CB A:SER228 4.2 48.1 1.0 C A:SER302 4.3 34.4 1.0 CB A:ALA263 4.3 24.3 1.0 CA A:SER265 4.4 29.2 1.0 CA A:GLY303 4.5 34.0 1.0 CB A:TYR301 4.6 32.9 1.0 N A:SER302 4.6 31.5 1.0 CA A:ALA263 4.6 29.7 1.0 CA A:TYR301 4.6 36.5 1.0 O A:LEU299 4.7 38.4 1.0 N A:VAL304 4.7 32.6 1.0 O A:SER302 4.7 34.1 1.0 CA A:SER302 4.7 33.4 1.0 OE2 A:GLU251 4.7 40.4 1.0 CB A:VAL304 4.8 34.0 1.0 CD2 A:TYR301 4.8 34.7 1.0 N A:TYR301 4.9 41.0 1.0 CA A:VAL304 4.9 33.0 1.0 N A:ALA264 4.9 28.2 1.0 N A:GLY229 4.9 31.6 1.0

Potassium binding site 2 out of 2 in the Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Engineered Holo Tryptophan Synthase (TM9D8*) Derived From T. Maritima Trpb within 5.0Å range: probe atom residue distance (Å) B Occ B:K402 b:44.9 occ:1.00 O B:HOH506 2.6 46.3 1.0 O B:TYR301 2.6 38.1 1.0 O B:GLY303 2.7 39.1 1.0 O B:ALA263 2.7 45.1 1.0 OG B:SER265 2.8 44.6 1.0 CB B:SER265 3.7 43.2 1.0 C B:TYR301 3.7 46.8 1.0 C B:GLY303 3.7 36.8 1.0 O B:SER228 3.8 46.9 1.0 OG B:SER228 3.8 55.0 1.0 O B:HOH512 3.8 48.2 1.0 C B:ALA263 3.9 40.9 1.0 N B:SER265 4.0 42.0 1.0 C B:SER228 4.1 41.3 1.0 N B:GLY303 4.1 36.5 1.0 CA B:SER228 4.2 47.0 1.0 CB B:ALA263 4.2 43.4 1.0 C B:SER302 4.2 41.2 1.0 CB B:TYR301 4.4 39.4 1.0 CA B:GLY303 4.4 32.2 1.0 CA B:SER265 4.5 48.6 1.0 CA B:TYR301 4.5 43.3 1.0 CA B:ALA263 4.5 40.5 1.0 O B:SER302 4.5 42.6 1.0 N B:SER302 4.5 43.5 1.0 CB B:SER228 4.6 50.0 1.0 CA B:SER302 4.7 38.2 1.0 N B:VAL304 4.7 35.4 1.0 CD2 B:TYR301 4.7 38.6 1.0 OE2 B:GLU251 4.7 61.3 1.0 O B:LEU299 4.7 54.1 1.0 N B:TYR301 4.8 43.8 1.0 CB B:VAL304 4.8 37.7 1.0 N B:ALA264 4.9 41.2 1.0 CA B:VAL304 4.9 32.4 1.0 CG B:TYR301 5.0 39.8 1.0

K.E.Johnston, P.J.Almhjell, E.J.Watkins-Dulaney, G.Liu, N.J.Porter, J.Yang, F.H.Arnold. A Combinatorially Complete Epistatic Fitness Landscape in An Enzyme Active Site. Proc.Natl.Acad.Sci.Usa V. 121 39121 2024.
ISSN: ESSN 1091-6490
PubMed: 39074291
DOI: 10.1073/PNAS.2400439121