Potassium in PDB 6dur: Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with L- Phenylalanine

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

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with L- Phenylalanine, PDB code: 6dur 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)	48.73 / 1.80
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.510, 133.330, 142.840, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 19.3

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase Complexed with L- Phenylalanine (pdb code 6dur). 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 Complexed with L- Phenylalanine, PDB code: 6dur:
Jump to Potassium binding site number: 1; 2;

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


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 Complexed with L- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:31.7 occ:1.00 O A:HOH685 2.7 27.5 1.0 OE1 A:GLU69 2.7 26.7 1.0 O B:HOH691 2.8 28.5 1.0 O B:GLY52 2.8 28.1 1.0 O B:ASN262 2.9 27.1 1.0 O B:HOH780 3.0 33.0 1.0 O A:GLU69 3.4 29.3 1.0 C B:GLY52 3.6 30.0 1.0 CB A:GLU69 3.8 24.2 1.0 CD A:GLU69 3.9 29.2 1.0 CA B:GLY52 3.9 31.6 1.0 C B:ASN262 3.9 28.9 1.0 CB B:ASN262 4.0 26.1 1.0 CA A:GLU69 4.1 29.1 1.0 CA B:ASN262 4.1 22.5 1.0 C A:GLU69 4.1 30.6 1.0 CA A:ALA295 4.3 29.1 1.0 CG A:GLU69 4.3 26.3 1.0 O A:HOH721 4.4 28.5 1.0 N A:GLY296 4.4 26.6 1.0 N B:THR53 4.7 29.9 1.0 CB A:ALA295 4.8 28.7 1.0 O A:LEU294 4.8 28.1 1.0 O B:SER51 4.8 28.1 1.0 ND2 B:ASN262 4.9 27.9 1.0 CE B:LYS256 4.9 29.4 1.0 C A:ALA295 4.9 24.6 1.0 CG B:ASN262 4.9 30.4 1.0 OE2 A:GLU69 5.0 27.1 1.0

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


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 Complexed with L- Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:K503 b:29.2 occ:1.00 OE1 B:GLU69 2.7 25.6 1.0 O A:GLY52 2.8 28.4 1.0 O A:HOH707 2.8 28.3 1.0 O B:HOH690 2.8 29.9 1.0 O A:ASN262 3.0 29.2 1.0 O A:HOH706 3.1 36.4 1.0 O B:GLU69 3.3 31.0 1.0 C A:GLY52 3.5 31.3 1.0 CB B:GLU69 3.7 25.8 1.0 CD B:GLU69 3.9 28.6 1.0 CA A:GLY52 3.9 28.4 1.0 CB A:ASN262 3.9 26.3 1.0 C A:ASN262 3.9 26.4 1.0 CA B:GLU69 4.0 24.1 1.0 C B:GLU69 4.0 27.6 1.0 CA A:ASN262 4.1 27.1 1.0 CG B:GLU69 4.3 27.2 1.0 O B:HOH740 4.3 32.7 1.0 CA B:ALA295 4.4 29.4 1.0 N B:GLY296 4.5 30.7 1.0 N A:THR53 4.7 26.8 1.0 ND2 A:ASN262 4.8 26.9 1.0 CE A:LYS256 4.8 31.1 1.0 CG A:ASN262 4.8 26.1 1.0 O B:LEU294 4.9 29.3 1.0 O A:SER51 4.9 30.6 1.0 CB B:ALA295 4.9 27.7 1.0 OE2 B:GLU69 4.9 23.0 1.0 C B:ALA295 5.0 31.2 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