Potassium in PDB 6dyt: 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: 6dyt 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)	37.89 / 2.05
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.640, 133.270, 145.070, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 23.2

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Alanine (pdb code 6dyt). 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: 6dyt:
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:58.6 occ:1.00 OE1 B:GLU69 2.8 50.9 1.0 O A:GLY52 2.8 53.6 1.0 O B:HOH1631 2.8 53.7 1.0 O B:HOH1663 2.9 50.1 1.0 O A:HOH673 2.9 63.7 1.0 O A:ASN262 3.0 48.7 1.0 O B:GLU69 3.1 59.2 1.0 C A:GLY52 3.6 54.2 1.0 CB B:GLU69 3.7 49.6 1.0 C B:GLU69 3.8 55.7 1.0 CD B:GLU69 3.9 52.8 1.0 CB A:ASN262 3.9 54.3 1.0 CA B:GLU69 3.9 56.4 1.0 CA A:GLY52 3.9 60.9 1.0 C A:ASN262 4.0 39.5 1.0 CA A:ASN262 4.2 51.6 1.0 CG B:GLU69 4.2 51.9 1.0 O B:HOH1649 4.3 52.9 1.0 CA B:ALA295 4.5 53.3 1.0 N B:GLY296 4.5 56.9 1.0 N A:THR53 4.7 51.3 1.0 CE A:LYS256 4.8 61.0 1.0 ND2 A:ASN262 4.8 50.1 1.0 CG A:ASN262 4.8 52.4 1.0 O B:LEU294 4.9 65.5 1.0 O A:SER51 4.9 59.0 1.0 CB B:ALA295 4.9 49.3 1.0 O B:ALA70 5.0 56.5 1.0 OE2 B:GLU69 5.0 45.8 1.0 NZ A:LYS256 5.0 55.2 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:K502 b:61.7 occ:1.00 O B:GLY52 2.8 45.9 1.0 OE1 A:GLU69 2.8 57.2 1.0 O A:HOH678 2.8 47.2 1.0 O A:HOH635 2.9 53.0 1.0 O B:HOH1702 3.0 59.1 1.0 O B:ASN262 3.1 49.7 1.0 O A:GLU69 3.2 71.7 1.0 C B:GLY52 3.6 55.7 1.0 CB A:GLU69 3.7 52.2 1.0 CD A:GLU69 3.8 61.5 1.0 CB B:ASN262 3.9 43.8 1.0 CA A:GLU69 3.9 58.2 1.0 C A:GLU69 3.9 65.9 1.0 CA B:GLY52 3.9 62.7 1.0 C B:ASN262 4.0 50.9 1.0 CA B:ASN262 4.2 45.2 1.0 CG A:GLU69 4.2 57.5 1.0 O A:HOH657 4.3 49.5 1.0 CA A:ALA295 4.4 51.9 1.0 N A:GLY296 4.5 47.9 1.0 N B:THR53 4.7 49.5 1.0 ND2 B:ASN262 4.7 49.9 1.0 CB A:ALA295 4.8 50.3 1.0 CG B:ASN262 4.8 54.8 1.0 CE B:LYS256 4.9 56.7 1.0 O B:SER51 4.9 62.5 1.0 OE2 A:GLU69 5.0 54.1 1.0 O A:LEU294 5.0 55.2 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