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

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

The structure of Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Methionine, PDB code: 6ecg 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)	45.95 / 2.27
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.610, 132.850, 144.270, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22

The binding sites of Potassium atom in the Citrobacter Freundii Tyrosine Phenol-Lyase F448A Mutant Complexed with L-Methionine (pdb code 6ecg). 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-Methionine, PDB code: 6ecg:
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-Methionine


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-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:K501 b:35.6 occ:1.00 OE1 B:GLU69 2.8 29.6 1.0 O A:GLY52 2.8 33.4 1.0 O B:HOH525 2.8 30.0 1.0 O B:HOH599 2.8 29.8 1.0 O A:HOH724 2.9 38.6 1.0 O A:ASN262 3.0 28.3 1.0 O B:GLU69 3.1 42.9 1.0 C A:GLY52 3.6 40.0 1.0 CB B:GLU69 3.7 34.0 1.0 CB A:ASN262 3.8 32.2 1.0 C B:GLU69 3.8 44.4 1.0 CA B:GLU69 3.8 38.5 1.0 CD B:GLU69 3.9 36.5 1.0 C A:ASN262 3.9 33.7 1.0 CA A:GLY52 4.0 36.8 1.0 CA A:ASN262 4.1 33.6 1.0 O B:HOH522 4.2 24.2 1.0 CG B:GLU69 4.3 30.1 1.0 CA B:ALA295 4.4 36.9 1.0 N B:GLY296 4.4 33.9 1.0 N A:THR53 4.7 38.4 1.0 CG A:ASN262 4.8 37.5 1.0 CE A:LYS256 4.8 32.9 1.0 ND2 A:ASN262 4.8 27.6 1.0 CB B:ALA295 4.8 28.4 1.0 O B:LEU294 4.9 39.7 1.0 C B:ALA295 4.9 38.0 1.0 O B:ALA70 4.9 34.0 1.0 OE2 B:GLU69 4.9 28.5 1.0 O A:SER51 4.9 43.3 1.0

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


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-Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:34.0 occ:1.00 O B:GLY52 2.7 36.8 1.0 O A:HOH728 2.7 29.5 1.0 OE1 A:GLU69 2.8 30.5 1.0 O A:HOH657 2.9 35.7 1.0 O B:HOH600 2.9 40.6 1.0 O B:ASN262 3.0 28.7 1.0 O A:GLU69 3.2 40.2 1.0 C B:GLY52 3.5 37.5 1.0 CB A:GLU69 3.7 39.8 1.0 CA B:GLY52 3.9 39.3 1.0 CD A:GLU69 3.9 35.3 1.0 CA A:GLU69 3.9 49.8 1.0 C A:GLU69 3.9 45.1 1.0 CB B:ASN262 3.9 33.9 1.0 C B:ASN262 4.0 31.4 1.0 CA B:ASN262 4.2 30.1 1.0 O A:HOH631 4.2 27.7 1.0 CG A:GLU69 4.2 32.8 1.0 CA A:ALA295 4.3 38.1 1.0 N A:GLY296 4.5 34.9 1.0 N B:THR53 4.7 33.5 1.0 ND2 B:ASN262 4.7 34.3 1.0 CB A:ALA295 4.7 28.3 1.0 CG B:ASN262 4.8 34.5 1.0 O A:LEU294 4.9 35.8 1.0 CE B:LYS256 4.9 33.1 1.0 OE2 A:GLU69 5.0 33.5 1.0 C A:ALA295 5.0 34.9 1.0 O B:SER51 5.0 45.4 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