Potassium in PDB 2ez2: Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0

All present enzymatic activity of Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0:
4.1.99.2;

The structure of Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0, PDB code: 2ez2 was solved by D.Milic, D.Matkovic-Calogovic, T.V.Demidkina, A.A.Antson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.74 / 1.85
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	133.644, 143.735, 59.915, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 20.6

The binding sites of Potassium atom in the Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0 (pdb code 2ez2). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0, PDB code: 2ez2:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:K1500 b:16.3 occ:1.00 OE1 B:GLU69 2.7 15.4 1.0 O A:HOH1622 2.8 17.1 1.0 O A:GLY52 2.8 12.0 1.0 O B:HOH5602 2.8 14.6 1.0 O A:ASN262 3.1 22.0 1.0 O A:HOH1671 3.2 23.2 1.0 O B:GLU69 3.3 16.9 1.0 C A:GLY52 3.7 13.0 1.0 CB B:GLU69 3.7 12.7 1.0 CD B:GLU69 3.9 13.6 1.0 CA B:GLU69 3.9 14.1 1.0 C B:GLU69 3.9 15.3 1.0 CA A:GLY52 4.0 12.7 1.0 C A:ASN262 4.0 19.4 1.0 CB A:ASN262 4.0 15.7 1.0 O B:HOH5631 4.1 17.4 1.0 CA A:ASN262 4.2 18.4 1.0 CG B:GLU69 4.3 17.1 1.0 CA B:ALA295 4.4 18.6 1.0 N B:GLY296 4.5 16.3 1.0 N A:THR53 4.7 13.2 1.0 ND2 A:ASN262 4.8 13.6 1.0 CB B:ALA295 4.8 17.2 1.0 CG A:ASN262 4.9 17.7 1.0 OE2 B:GLU69 4.9 15.7 1.0 CE A:LYS256 4.9 19.4 1.0 O B:ALA70 4.9 18.8 1.0 O B:LEU294 5.0 19.0 1.0 O A:SER51 5.0 13.2 1.0 C B:ALA295 5.0 18.7 1.0

Potassium binding site 2 out of 2 in the Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Apo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0 within 5.0Å range: probe atom residue distance (Å) B Occ B:K5500 b:17.2 occ:1.00 O A:HOH1618 2.6 15.2 1.0 OE1 A:GLU69 2.8 16.8 1.0 O B:GLY52 2.8 13.8 1.0 O B:HOH5613 2.9 16.4 1.0 O B:ASN262 3.0 18.7 1.0 O B:HOH5661 3.0 21.6 1.0 O A:GLU69 3.4 15.1 1.0 C B:GLY52 3.6 14.8 1.0 CB A:GLU69 3.8 14.2 1.0 CD A:GLU69 3.9 19.1 1.0 CA B:GLY52 3.9 14.3 1.0 C B:ASN262 4.0 20.5 1.0 CB B:ASN262 4.0 17.0 1.0 C A:GLU69 4.1 14.8 1.0 CA A:GLU69 4.1 13.5 1.0 CA B:ASN262 4.2 18.8 1.0 O A:HOH1605 4.2 13.1 1.0 CA A:ALA295 4.3 17.3 1.0 CG A:GLU69 4.4 16.1 1.0 N A:GLY296 4.5 14.8 1.0 N B:THR53 4.8 14.8 1.0 O A:LEU294 4.8 18.1 1.0 CB A:ALA295 4.8 17.1 1.0 CE B:LYS256 4.8 18.3 1.0 ND2 B:ASN262 4.9 17.9 1.0 O B:SER51 4.9 14.8 1.0 C A:ALA295 4.9 18.0 1.0 OE2 A:GLU69 4.9 16.5 1.0 CG B:ASN262 5.0 20.4 1.0

D.Milic, D.Matkovic-Calogovic, T.V.Demidkina, V.V.Kulikova, N.I.Sinitzina, A.A.Antson. Structures of Apo- and Holo-Tyrosine Phenol-Lyase Reveal A Catalytically Critical Closed Conformation and Suggest A Mechanism For Activation By K+ Ions Biochemistry V. 45 7544 2006.
ISSN: ISSN 0006-2960
PubMed: 16768450
DOI: 10.1021/BI0601858