Potassium in PDB 6dz5: Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine

All present enzymatic activity of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine:
4.1.99.2;

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine, PDB code: 6dz5 was solved by R.S.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.47 / 2.26
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.880, 132.810, 145.370, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.1

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine (pdb code 6dz5). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine, PDB code: 6dz5:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:54.4 occ:1.00 O A:GLY52 2.7 41.7 1.0 OE2 B:GLU69 2.8 40.3 1.0 O B:HOH788 2.8 45.6 1.0 O B:HOH758 2.8 42.8 1.0 O A:HOH663 2.9 57.7 1.0 O B:GLU69 3.1 50.9 1.0 O A:ASN262 3.1 42.6 1.0 C A:GLY52 3.6 45.9 1.0 CB B:GLU69 3.7 43.1 1.0 C B:GLU69 3.8 52.4 1.0 CA B:GLU69 3.8 47.8 1.0 CD B:GLU69 3.9 45.8 1.0 CA A:GLY52 3.9 46.3 1.0 CB A:ASN262 3.9 42.1 1.0 C A:ASN262 4.0 38.3 1.0 CA A:ASN262 4.2 39.8 1.0 O B:HOH751 4.2 38.6 1.0 CG B:GLU69 4.3 35.6 1.0 CA B:ALA295 4.5 42.6 1.0 N B:GLY296 4.6 43.4 1.0 N A:THR53 4.7 44.0 1.0 ND2 A:ASN262 4.8 46.5 1.0 CG A:ASN262 4.8 51.8 1.0 CE A:LYS256 4.9 39.4 1.0 CB B:ALA295 4.9 36.1 1.0 O A:SER51 4.9 48.3 1.0 OE1 B:GLU69 5.0 45.6 1.0

Potassium binding site 2 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:50.7 occ:1.00 O A:HOH711 2.8 36.8 1.0 O B:GLY52 2.8 40.1 1.0 OE1 A:GLU69 2.8 48.0 1.0 O A:HOH636 2.9 46.1 1.0 O B:HOH807 2.9 54.3 1.0 O B:ASN262 3.0 37.6 1.0 O A:GLU69 3.1 64.6 1.0 C B:GLY52 3.6 42.6 1.0 CB A:GLU69 3.7 42.6 1.0 CB B:ASN262 3.9 37.5 1.0 CA A:GLU69 3.9 53.8 1.0 C A:GLU69 3.9 60.0 1.0 CD A:GLU69 3.9 58.1 1.0 CA B:GLY52 4.0 42.4 1.0 C B:ASN262 4.0 44.0 1.0 CA B:ASN262 4.2 42.4 1.0 CG A:GLU69 4.3 53.0 1.0 O A:HOH619 4.3 41.3 1.0 CA A:ALA295 4.4 43.2 1.0 N A:GLY296 4.6 44.0 1.0 N B:THR53 4.7 43.6 1.0 ND2 B:ASN262 4.7 41.3 1.0 CG B:ASN262 4.8 44.8 1.0 CB A:ALA295 4.8 36.0 1.0 CE B:LYS256 4.9 46.7 1.0 O B:SER51 5.0 46.1 1.0 O A:LEU294 5.0 54.0 1.0

R.S.Phillips, S.Craig. Crystal Structures of Wild-Type and F448A Mutant Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with A Substrate and Inhibitors: Implications For the Reaction Mechanism. Biochemistry V. 57 6166 2018.
ISSN: ISSN 1520-4995
PubMed: 30260636
DOI: 10.1021/ACS.BIOCHEM.8B00724