Potassium in PDB 2yhk: D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii

All present enzymatic activity of D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii:
4.1.99.2;

The structure of D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii, PDB code: 2yhk was solved by D.Milic, T.V.Demidkina, D.Matkovic-Calogovic, A.A.Antson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.91
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	132.605, 142.705, 59.412, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 17.7

The binding sites of Potassium atom in the D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii (pdb code 2yhk). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii, PDB code: 2yhk:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii within 5.0Å range: probe atom residue distance (Å) B Occ A:K500 b:23.7 occ:1.00 O B:HOH2246 2.7 12.3 1.0 OE1 B:GLU69 2.8 20.4 1.0 O A:ASN262 2.8 19.9 1.0 O A:GLY52 2.8 17.2 1.0 O A:HOH2082 2.9 17.8 1.0 O A:HOH2263 3.1 21.5 1.0 O B:GLU69 3.5 21.5 1.0 C A:GLY52 3.6 18.0 1.0 C A:ASN262 3.8 19.4 1.0 CA A:GLY52 3.8 20.6 1.0 CB B:GLU69 3.9 18.4 1.0 CD B:GLU69 3.9 18.2 1.0 CB A:ASN262 4.0 18.0 1.0 CA A:ASN262 4.1 16.8 1.0 CA B:GLU69 4.1 20.0 1.0 C B:GLU69 4.2 20.9 1.0 CA B:ALA295 4.2 20.3 1.0 O B:HOH2085 4.4 10.9 1.0 CG B:GLU69 4.4 17.6 1.0 N B:GLY296 4.4 19.6 1.0 O B:LEU294 4.7 22.9 1.0 N A:THR53 4.7 18.1 1.0 CE A:LYS256 4.8 21.1 1.0 CB B:ALA295 4.8 21.0 1.0 C B:ALA295 4.9 20.6 1.0 OE2 B:GLU69 4.9 18.7 1.0 CG A:ASN262 5.0 17.5 1.0 O A:SER51 5.0 20.6 1.0 ND2 A:ASN262 5.0 16.5 1.0 N A:ILE263 5.0 18.0 1.0

Potassium binding site 2 out of 2 in the D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of D214A Mutant of Tyrosine Phenol-Lyase From Citrobacter Freundii within 5.0Å range: probe atom residue distance (Å) B Occ B:K500 b:24.5 occ:1.00 OE1 A:GLU69 2.7 17.3 1.0 O A:HOH2283 2.7 13.2 1.0 O B:GLY52 2.8 19.9 1.0 O B:ASN262 2.9 20.1 1.0 O A:HOH2103 2.9 14.5 1.0 O B:HOH2236 3.1 15.8 1.0 O A:GLU69 3.4 22.1 1.0 C B:GLY52 3.6 19.6 1.0 CD A:GLU69 3.8 21.5 1.0 CA B:GLY52 3.9 20.6 1.0 CB A:GLU69 3.9 19.1 1.0 C B:ASN262 3.9 19.9 1.0 CB B:ASN262 4.0 19.8 1.0 CA A:GLU69 4.1 20.0 1.0 C A:GLU69 4.1 22.1 1.0 CA B:ASN262 4.2 18.4 1.0 CA A:ALA295 4.3 19.7 1.0 CG A:GLU69 4.3 19.9 1.0 O A:HOH2098 4.4 12.2 1.0 N A:GLY296 4.4 17.9 1.0 N B:THR53 4.7 19.9 1.0 O A:LEU294 4.8 20.9 1.0 CB A:ALA295 4.8 17.0 1.0 ND2 B:ASN262 4.9 20.6 1.0 C A:ALA295 4.9 20.3 1.0 OE2 A:GLU69 4.9 17.2 1.0 CE B:LYS256 4.9 17.8 1.0 CG B:ASN262 4.9 23.4 1.0 O B:SER51 5.0 20.7 1.0

D.Milic, T.V.Demidkina, L.N.Zakomirdina, D.Matkovic-Calogovic, A.A.Antson. Crystal Structure of Citrobacter Freundii ASP214ALA Tyrosine Phenol-Lyase Reveals That ASP214 Is Critical For Maintaining A Strain in the Internal Aldimine Croatica Chemica Acta V. 85 283 2012.
ISSN: ISSN 0011-1643
DOI: 10.5562/CCA1915