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

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

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Phenylalanine, PDB code: 6dvx 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)	37.75 / 2.27
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.780, 132.670, 144.970, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 21.9

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Phenylalanine (pdb code 6dvx). 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-Phenylalanine, PDB code: 6dvx:
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-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 F448A Mutant Complexed with L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:60.1 occ:1.00 O A:GLY52 2.8 59.0 1.0 OE1 B:GLU69 2.8 58.1 1.0 O B:HOH662 2.8 48.3 1.0 O A:HOH632 3.0 56.1 1.0 O A:ASN262 3.0 46.9 1.0 O A:HOH616 3.2 55.9 1.0 O B:GLU69 3.6 65.3 1.0 C A:GLY52 3.6 60.8 1.0 CB B:GLU69 3.8 48.3 1.0 CB A:ASN262 3.8 50.4 1.0 CA A:GLY52 3.9 67.4 1.0 CD B:GLU69 3.9 61.0 1.0 C A:ASN262 3.9 49.4 1.0 CA B:GLU69 4.0 60.9 1.0 CA A:ASN262 4.1 48.5 1.0 C B:GLU69 4.1 61.6 1.0 CG B:GLU69 4.4 54.2 1.0 O B:HOH643 4.4 46.2 1.0 CA B:ALA295 4.4 60.9 1.0 N B:GLY296 4.5 56.7 1.0 CE A:LYS256 4.7 56.4 1.0 ND2 A:ASN262 4.7 48.9 1.0 N A:THR53 4.7 57.7 1.0 CG A:ASN262 4.8 54.0 1.0 NZ A:LYS256 4.8 54.5 1.0 CB B:ALA295 4.9 50.9 1.0 O B:LEU294 4.9 58.8 1.0 O A:SER51 5.0 65.3 1.0 OE2 B:GLU69 5.0 56.7 1.0 C B:ALA295 5.0 55.1 1.0

Potassium binding site 2 out of 2 in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant 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 F448A Mutant Complexed with L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ A:K504 b:63.1 occ:1.00 O B:GLY52 2.8 59.6 1.0 O A:HOH706 2.8 52.0 1.0 OE1 A:GLU69 2.8 54.8 1.0 O B:HOH670 2.9 53.7 1.0 O B:ASN262 2.9 48.4 1.0 O B:HOH652 3.1 56.2 1.0 O A:GLU69 3.5 68.4 1.0 C B:GLY52 3.6 58.1 1.0 CB A:GLU69 3.7 56.9 1.0 CB B:ASN262 3.7 45.8 1.0 C B:ASN262 3.9 55.2 1.0 CD A:GLU69 3.9 70.6 1.0 CA B:GLY52 3.9 64.0 1.0 CA A:GLU69 4.0 62.8 1.0 CA B:ASN262 4.1 52.2 1.0 C A:GLU69 4.1 64.8 1.0 CG A:GLU69 4.3 56.0 1.0 O A:HOH643 4.3 50.2 1.0 CA A:ALA295 4.3 62.1 1.0 N A:GLY296 4.5 52.7 1.0 ND2 B:ASN262 4.6 44.3 1.0 CG B:ASN262 4.7 47.7 1.0 N B:THR53 4.7 57.0 1.0 CE B:LYS256 4.8 47.1 1.0 CB A:ALA295 4.8 53.4 1.0 O A:LEU294 4.9 66.8 1.0 O B:SER51 5.0 62.3 1.0 OE2 A:GLU69 5.0 52.0 1.0 C A:ALA295 5.0 52.5 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