Potassium in PDB 6dxv: Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant

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

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant, PDB code: 6dxv 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)	37.48 / 2.20
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.350, 132.180, 145.010, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 25

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant (pdb code 6dxv). 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, PDB code: 6dxv:
Jump to Potassium binding site number: 1; 2;

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:70.0 occ:1.00 O A:GLY52 2.7 55.7 1.0 O A:HOH624 2.8 78.8 1.0 OE1 B:GLU69 2.8 55.6 1.0 O B:HOH612 2.8 58.5 1.0 O A:HOH628 3.1 71.7 1.0 O A:ASN262 3.1 54.4 1.0 O B:GLU69 3.2 67.5 1.0 C A:GLY52 3.6 62.1 1.0 CB B:GLU69 3.8 55.3 1.0 CA A:GLY52 3.9 61.3 1.0 CD B:GLU69 3.9 69.3 1.0 C B:GLU69 3.9 64.7 1.0 CA B:GLU69 3.9 67.1 1.0 CB A:ASN262 4.0 54.9 1.0 C A:ASN262 4.1 57.3 1.0 O B:HOH657 4.1 55.0 1.0 CA A:ASN262 4.3 55.3 1.0 CG B:GLU69 4.3 53.2 1.0 CA B:ALA295 4.4 56.0 1.0 N B:GLY296 4.5 51.9 1.0 N A:THR53 4.6 56.2 1.0 CB B:ALA295 4.8 54.7 1.0 O A:SER51 4.9 67.3 1.0 O B:LEU294 5.0 67.9 1.0 CG A:ASN262 5.0 59.3 1.0 OE2 B:GLU69 5.0 67.6 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:K501 b:69.6 occ:1.00 O B:GLY52 2.7 56.9 1.0 O A:HOH689 2.8 63.7 1.0 OE1 A:GLU69 2.9 55.1 1.0 O B:ASN262 2.9 62.1 1.0 O B:HOH634 3.0 85.7 1.0 O A:HOH678 3.0 79.5 1.0 C B:GLY52 3.6 58.8 1.0 O A:GLU69 3.6 71.0 1.0 CB B:ASN262 3.8 54.0 1.0 CA B:GLY52 3.8 63.4 1.0 C B:ASN262 3.9 59.0 1.0 CB A:GLU69 3.9 53.0 1.0 CD A:GLU69 3.9 69.9 1.0 CA B:ASN262 4.1 56.6 1.0 O A:HOH685 4.2 72.2 1.0 CA A:GLU69 4.2 51.4 1.0 C A:GLU69 4.2 61.9 1.0 CA A:ALA295 4.3 62.5 1.0 CG A:GLU69 4.4 60.6 1.0 N A:GLY296 4.6 56.3 1.0 N B:THR53 4.7 60.2 1.0 CB A:ALA295 4.8 61.3 1.0 CG B:ASN262 4.8 59.5 1.0 ND2 B:ASN262 4.9 50.0 1.0 O A:LEU294 4.9 72.6 1.0 O B:SER51 5.0 66.7 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