Potassium in PDB 2ez1: Holo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0

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

The structure of Holo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0, PDB code: 2ez1 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)	19.84 / 1.90
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	133.860, 143.850, 60.070, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18.6

The binding sites of Potassium atom in the Holo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0 (pdb code 2ez1). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Holo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0, PDB code: 2ez1:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Holo 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 Holo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:K500 b:16.3 occ:1.00 O A:GLY52 2.7 14.3 1.0 OE1 B:GLU69 2.8 18.6 1.0 O A:ASN262 2.8 23.3 1.0 O B:HOH501 2.8 11.9 1.0 O B:HOH535 2.9 15.1 1.0 O A:HOH510 3.0 16.7 1.0 C A:GLY52 3.6 14.6 1.0 O B:GLU69 3.7 22.5 1.0 C A:ASN262 3.8 21.5 1.0 CB B:GLU69 3.9 19.1 1.0 CD B:GLU69 3.9 21.1 1.0 CA A:GLY52 3.9 13.7 1.0 CB A:ASN262 4.0 19.0 1.0 CA A:ASN262 4.1 21.4 1.0 CA B:GLU69 4.2 20.7 1.0 CA B:ALA295 4.2 19.9 1.0 C B:GLU69 4.3 22.3 1.0 O B:HOH518 4.4 12.3 1.0 CG B:GLU69 4.4 19.6 1.0 N B:GLY296 4.5 20.4 1.0 CE A:LYS256 4.6 19.2 1.0 N A:THR53 4.7 14.9 1.0 O B:LEU294 4.8 22.5 1.0 CB B:ALA295 4.8 17.6 1.0 ND2 A:ASN262 4.9 18.8 1.0 C B:ALA295 4.9 21.2 1.0 OE2 B:GLU69 4.9 21.1 1.0 CG A:ASN262 4.9 22.8 1.0 O A:SER51 5.0 15.6 1.0

Potassium binding site 2 out of 2 in the Holo 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 Holo Tyrosine Phenol-Lyase From Citrobacter Freundii at pH 8.0 within 5.0Å range: probe atom residue distance (Å) B Occ B:K500 b:15.5 occ:1.00 O A:HOH504 2.7 12.4 1.0 OE1 A:GLU69 2.8 20.6 1.0 O B:GLY52 2.8 11.5 1.0 O B:ASN262 2.9 20.6 1.0 O B:HOH519 2.9 15.3 1.0 O B:HOH516 3.0 15.5 1.0 C B:GLY52 3.6 11.0 1.0 O A:GLU69 3.8 20.9 1.0 C B:ASN262 3.9 21.4 1.0 CB A:GLU69 3.9 21.1 1.0 CD A:GLU69 3.9 22.8 1.0 CA B:GLY52 4.0 11.5 1.0 CB B:ASN262 4.0 18.4 1.0 CA B:ASN262 4.2 19.1 1.0 CA A:ALA295 4.2 20.6 1.0 CA A:GLU69 4.2 21.0 1.0 C A:GLU69 4.4 21.6 1.0 CG A:GLU69 4.4 20.8 1.0 N A:GLY296 4.4 21.1 1.0 O A:HOH520 4.5 15.6 1.0 CE B:LYS256 4.6 19.8 1.0 N B:THR53 4.7 11.6 1.0 CB A:ALA295 4.7 19.7 1.0 O A:LEU294 4.8 20.7 1.0 C A:ALA295 4.8 22.0 1.0 ND2 B:ASN262 4.9 19.7 1.0 O B:SER51 4.9 14.0 1.0 OE2 A:GLU69 5.0 19.1 1.0 CG B:ASN262 5.0 21.4 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