Caesium in PDB 3ump: Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Cesium and Atp

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

The structure of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Cesium and Atp, PDB code: 3ump 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)	49.05 / 1.85
Space group	P 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	43.856, 88.914, 176.405, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 20.9

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

Magnesium

(Mg)

4 atoms

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

Caesium binding site 1 out of 2 in the Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Cesium and Atp


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Cesium and Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cs315 b:25.4 occ:1.00 O A:ALA286 3.0 36.1 1.0 O A:VAL252 3.0 72.8 1.0 O A:ASN289 3.0 51.0 1.0 O A:GLY291 3.0 42.2 1.0 O A:ARG293 3.1 52.9 1.0 O A:SER250 3.2 32.8 1.0 OG A:SER250 3.8 29.0 1.0 C A:ASN289 3.9 44.5 1.0 C A:ALA286 4.0 24.8 1.0 CB A:SER250 4.0 34.2 1.0 C A:GLY291 4.0 42.9 1.0 C A:SER250 4.0 31.3 1.0 C A:VAL252 4.0 45.1 1.0 N A:ARG293 4.1 31.6 1.0 C A:ARG293 4.1 40.0 1.0 N A:VAL252 4.2 25.0 1.0 O A:GLN290 4.3 34.7 1.0 C A:THR292 4.3 31.5 1.0 CB A:ASN289 4.4 43.6 1.0 CA A:VAL252 4.5 28.0 1.0 C A:GLN290 4.5 30.8 1.0 CA A:ASN289 4.5 37.7 1.0 CB A:VAL252 4.5 26.9 1.0 CA A:THR287 4.5 20.4 1.0 CA A:SER250 4.6 32.8 1.0 CA A:THR292 4.6 37.0 1.0 CA A:ARG293 4.6 41.9 1.0 N A:ASN289 4.6 31.3 1.0 N A:THR292 4.6 35.8 1.0 N A:THR287 4.7 21.4 1.0 C A:THR251 4.7 24.9 1.0 N A:GLY291 4.8 37.5 1.0 C A:THR287 4.8 25.8 1.0 O A:THR292 4.8 34.9 1.0 N A:THR251 4.8 28.0 1.0 N A:GLN290 4.8 35.0 1.0 CA A:ALA286 4.9 21.1 1.0 O A:THR287 4.9 25.1 1.0 CA A:GLY291 5.0 43.5 1.0

Caesium binding site 2 out of 2 in the Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Cesium and Atp


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 2 of Crystal Structure of the Phosphofructokinase-2 From Escherichia Coli in Complex with Cesium and Atp within 5.0Å range: probe atom residue distance (Å) B Occ B:Cs315 b:24.8 occ:1.00 O B:ASN289 2.9 41.4 1.0 O B:VAL252 3.0 64.4 1.0 O B:GLY291 3.0 46.8 1.0 O B:ALA286 3.0 32.3 1.0 O B:ARG293 3.0 62.4 1.0 O B:SER250 3.4 30.7 1.0 OG B:SER250 3.8 29.0 1.0 CB B:SER250 3.8 38.3 1.0 C B:ASN289 3.9 40.6 1.0 C B:GLY291 4.0 42.2 1.0 C B:ALA286 4.0 22.2 1.0 C B:SER250 4.0 36.3 1.0 C B:VAL252 4.0 36.9 1.0 N B:ARG293 4.1 30.9 1.0 C B:ARG293 4.1 46.0 1.0 N B:VAL252 4.2 22.4 1.0 C B:THR292 4.3 34.3 1.0 CB B:ASN289 4.3 36.8 1.0 O B:GLN290 4.4 33.9 1.0 CB B:VAL252 4.4 31.7 1.0 CA B:VAL252 4.5 25.5 1.0 CA B:SER250 4.5 33.0 1.0 CA B:ASN289 4.5 33.0 1.0 C B:GLN290 4.5 35.4 1.0 CA B:THR287 4.6 21.9 1.0 CA B:THR292 4.6 38.1 1.0 CA B:ARG293 4.6 42.1 1.0 N B:THR292 4.6 35.4 1.0 N B:ASN289 4.7 27.1 1.0 N B:THR287 4.7 20.8 1.0 C B:THR251 4.7 20.7 1.0 N B:GLY291 4.8 31.6 1.0 N B:THR251 4.8 22.9 1.0 O B:THR292 4.8 34.4 1.0 N B:GLN290 4.8 33.1 1.0 C B:THR287 4.9 23.4 1.0 CA B:ALA286 4.9 20.0 1.0 O B:THR287 4.9 25.3 1.0 CA B:GLY291 5.0 34.0 1.0 N B:SER250 5.0 30.7 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