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Potassium in PDB 8egy: Engineered Holo Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb

Enzymatic activity of Engineered Holo Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb

All present enzymatic activity of Engineered Holo Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb:
4.2.1.20;

Protein crystallography data

The structure of Engineered Holo Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb, PDB code: 8egy 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) 38.80 / 2.05
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 164.606, 164.606, 83.139, 90, 90, 90
R / Rfree (%) 21.6 / 23.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Engineered Holo Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb (pdb code 8egy). 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 Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb, PDB code: 8egy:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 8egy

Go back to Potassium Binding Sites List in 8egy
Potassium binding site 1 out of 2 in the Engineered Holo Tyrosine Synthase (TMTYRS1) 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 Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K402

b:40.0
occ:1.00
O A:TYR301 2.6 37.1 1.0
O A:HOH513 2.7 41.3 1.0
O A:GLY303 2.7 36.1 1.0
O A:ALA263 2.8 37.9 1.0
OG A:SER265 2.8 45.6 1.0
O A:SER228 3.6 39.7 1.0
C A:TYR301 3.7 37.6 1.0
C A:GLY303 3.7 40.9 1.0
O A:HOH564 3.8 37.9 1.0
OG A:SER228 3.8 54.3 1.0
CB A:SER265 3.8 41.9 1.0
C A:ALA263 3.9 36.9 1.0
N A:GLY303 3.9 38.7 1.0
C A:SER228 3.9 31.4 1.0
CA A:SER228 4.0 41.2 1.0
N A:SER265 4.1 38.3 1.0
CB A:ALA263 4.2 30.0 1.0
C A:PRO302 4.2 42.5 1.0
CA A:GLY303 4.3 38.6 1.0
CA A:PRO302 4.5 38.1 1.0
CA A:ALA263 4.5 33.4 1.0
N A:PRO302 4.5 39.4 1.0
CB A:SER228 4.5 49.0 1.0
CA A:SER265 4.5 39.7 1.0
O A:LEU299 4.6 33.7 1.0
CB A:TYR301 4.6 40.2 1.0
CA A:TYR301 4.6 36.8 1.0
N A:VAL304 4.7 40.9 1.0
CD2 A:TYR301 4.7 42.3 1.0
O A:PRO302 4.7 40.0 1.0
OE1 A:GLU251 4.8 40.7 1.0
N A:TYR301 4.8 40.9 1.0
N A:GLY229 4.8 37.9 1.0
N A:ALA264 4.9 37.0 1.0
CB A:VAL304 4.9 39.8 1.0
CA A:VAL304 5.0 40.4 1.0

Potassium binding site 2 out of 2 in 8egy

Go back to Potassium Binding Sites List in 8egy
Potassium binding site 2 out of 2 in the Engineered Holo Tyrosine Synthase (TMTYRS1) 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 Tyrosine Synthase (TMTYRS1) Derived From T. Maritima Trpb within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K402

b:49.6
occ:1.00
O B:TYR301 2.6 44.7 1.0
O B:HOH506 2.6 53.1 1.0
O B:GLY303 2.7 47.1 1.0
OG B:SER265 2.9 56.2 1.0
O B:ALA263 2.9 51.9 1.0
O B:SER228 3.4 53.1 0.4
O B:SER228 3.5 53.1 0.6
C B:GLY303 3.6 51.1 1.0
C B:TYR301 3.7 46.0 1.0
O B:HOH532 3.8 51.1 1.0
CB B:SER265 3.8 54.2 1.0
N B:GLY303 3.8 45.0 1.0
OG B:SER228 3.9 59.6 0.6
C B:SER228 4.0 52.3 0.4
C B:ALA263 4.0 49.0 1.0
C B:SER228 4.0 52.4 0.6
CA B:SER228 4.1 53.8 0.6
CA B:SER228 4.1 53.8 0.4
C B:PRO302 4.1 51.4 1.0
N B:SER265 4.1 51.6 1.0
CA B:GLY303 4.3 43.4 1.0
CB B:ALA263 4.3 56.0 1.0
CA B:PRO302 4.4 47.8 1.0
N B:PRO302 4.5 46.6 1.0
CB B:TYR301 4.5 48.0 1.0
CA B:TYR301 4.6 42.1 1.0
O B:PRO302 4.6 54.3 1.0
CA B:SER265 4.6 60.0 1.0
CB B:SER228 4.6 53.3 0.6
CA B:ALA263 4.6 52.9 1.0
N B:VAL304 4.6 43.1 1.0
CB B:SER228 4.6 53.2 0.4
CD2 B:TYR301 4.7 46.1 1.0
O B:LEU299 4.7 51.3 1.0
OE1 B:GLU251 4.8 58.9 1.0
N B:TYR301 4.8 48.9 1.0
CB B:VAL304 4.9 44.5 1.0
CA B:VAL304 4.9 42.0 1.0
N B:ALA264 5.0 53.0 1.0

Reference:

N.J.Porter, P.J.Almhjell, F.H.Arnold. Noncanonical L-Tyrosine Synthesis By Evolved Tryptophan Synthases To Be Published.
Page generated: Thu Dec 28 07:05:44 2023

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