Potassium in PDB 3umo: Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium

All present enzymatic activity of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium:
2.7.1.11;

The structure of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium, PDB code: 3umo was solved by H.M.Pereira, A.Caniuguir, M.Baez, R.Cabrera, R.C.Garratt, J.Babul, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.97 / 1.70
Space group	P 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	43.812, 88.770, 176.120, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 20.8

The structure of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Potassium atom in the Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium (pdb code 3umo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium, PDB code: 3umo:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium within 5.0Å range: probe atom residue distance (Å) B Occ A:K314 b:20.8 occ:1.00 O A:ASN289 2.7 60.3 1.0 O A:GLY291 2.8 63.6 1.0 O A:VAL252 2.8 26.3 1.0 O A:ARG293 2.9 39.1 1.0 O A:ALA286 2.9 25.1 1.0 O A:SER250 3.1 29.6 1.0 OG A:SER250 3.6 28.9 1.0 C A:ASN289 3.8 50.7 1.0 C A:GLY291 3.9 43.5 1.0 C A:VAL252 3.9 26.0 1.0 C A:SER250 3.9 22.2 1.0 C A:ALA286 4.0 18.2 1.0 CB A:SER250 4.0 27.5 1.0 C A:ARG293 4.0 26.9 1.0 N A:ARG293 4.1 24.7 1.0 O A:GLN290 4.2 30.3 1.0 N A:VAL252 4.2 19.8 1.0 C A:THR292 4.3 29.6 1.0 C A:GLN290 4.3 31.8 1.0 CA A:VAL252 4.4 17.0 1.0 CB A:VAL252 4.4 22.0 1.0 CB A:ASN289 4.4 35.4 1.0 CA A:ASN289 4.5 38.9 1.0 CA A:ARG293 4.5 29.5 1.0 CA A:SER250 4.5 23.9 1.0 CA A:THR292 4.6 27.1 1.0 N A:GLY291 4.6 32.3 1.0 N A:THR292 4.6 26.7 1.0 CA A:THR287 4.6 22.4 1.0 N A:ASN289 4.6 31.0 1.0 N A:GLN290 4.7 32.8 1.0 C A:THR251 4.7 17.4 1.0 N A:THR287 4.7 17.7 1.0 O A:THR292 4.8 27.6 1.0 CA A:GLY291 4.8 36.0 1.0 N A:THR251 4.8 18.6 1.0 CA A:GLN290 4.9 32.6 1.0 CB A:ARG293 4.9 35.5 1.0 CA A:ALA286 4.9 18.8 1.0 C A:THR287 4.9 21.1 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Potassium within 5.0Å range: probe atom residue distance (Å) B Occ B:K314 b:19.5 occ:1.00 O B:ASN289 2.8 43.0 1.0 O B:GLY291 2.9 66.4 1.0 O B:ALA286 2.9 24.4 1.0 O B:ARG293 3.0 38.6 1.0 O B:SER250 3.1 26.4 1.0 O B:VAL252 3.2 25.9 1.0 OG B:SER250 3.6 24.7 1.0 C B:ASN289 3.8 33.8 1.0 C B:GLY291 3.9 45.0 1.0 C B:SER250 3.9 29.0 1.0 CB B:SER250 3.9 29.6 1.0 C B:ALA286 4.0 18.6 1.0 C B:ARG293 4.0 35.9 1.0 N B:ARG293 4.1 30.6 1.0 O B:GLN290 4.2 27.3 1.0 C B:VAL252 4.2 23.4 1.0 N B:VAL252 4.2 18.9 1.0 C B:THR292 4.3 28.8 1.0 CB B:ASN289 4.4 25.8 1.0 C B:GLN290 4.4 29.7 1.0 CA B:ASN289 4.5 24.8 1.0 CB B:VAL252 4.5 20.5 1.0 CA B:SER250 4.5 22.1 1.0 CA B:VAL252 4.5 17.9 1.0 CA B:ARG293 4.6 26.7 1.0 CA B:THR292 4.6 27.1 1.0 N B:ASN289 4.6 23.6 1.0 N B:THR292 4.6 32.9 1.0 CA B:THR287 4.6 19.5 1.0 C B:THR251 4.7 22.9 1.0 N B:GLY291 4.7 28.0 1.0 N B:THR287 4.7 15.4 1.0 N B:GLN290 4.8 30.4 1.0 N B:THR251 4.8 20.1 1.0 CA B:ALA286 4.8 19.2 1.0 O B:THR292 4.8 30.8 1.0 CA B:GLY291 4.9 33.8 1.0 C B:THR287 4.9 19.6 1.0 CB B:ARG293 5.0 28.4 1.0 CB B:ALA286 5.0 18.5 1.0

M.Baez, R.Cabrera, H.M.Pereira, A.Blanco, P.Villalobos, C.A.Ramirez-Sarmiento, A.Caniuguir, V.Guixe, R.C.Garratt, J.Babul. A Ribokinase Family Conserved Monovalent Cation Binding Site Enhances the Mgatp-Induced Inhibition in E. Coli Phosphofructokinase-2 Biophys.J. V. 105 185 2013.
ISSN: ISSN 0006-3495
PubMed: 23823238
DOI: 10.1016/J.BPJ.2013.05.028