Potassium in PDB 8cg2: Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07

All present enzymatic activity of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07:
3.3.1.1;

The structure of Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07, PDB code: 8cg2 was solved by P.H.Malecki, M.Gawel, M.Stepniewska, K.Brzezinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.72 / 1.37
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	142.744, 85.381, 111.474, 90, 122.25, 90
R / Rfree (%)	14.8 / 18.1

The binding sites of Potassium atom in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07 (pdb code 8cg2). 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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07, PDB code: 8cg2:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07


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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07 within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:14.2 occ:1.00 O A:HOH789 2.7 16.0 1.0 O A:THR380 2.7 14.0 1.0 O A:HIS382 2.8 15.0 1.0 OG1 A:THR380 2.8 15.9 1.0 O A:HOH809 2.8 14.3 1.0 O C:HOH844 3.0 16.0 1.0 OE1 A:GLN65 3.3 14.9 1.0 NE2 A:GLN65 3.4 13.0 1.0 CD A:GLN65 3.5 12.8 1.0 CB A:THR380 3.5 15.2 1.0 C A:THR380 3.6 16.4 1.0 C A:HIS382 3.6 13.7 1.0 O A:GLY381 3.8 15.2 1.0 CA A:PRO383 4.0 14.4 1.0 N6 A:ADE505 4.0 16.0 1.0 C A:GLY381 4.1 12.4 1.0 N A:PRO383 4.2 13.8 1.0 CA A:THR380 4.2 13.6 1.0 CB C:ASP216 4.2 14.1 1.0 O A:HOH933 4.4 17.5 1.0 N A:HIS382 4.5 13.3 1.0 CG C:ASP216 4.5 13.6 1.0 N A:GLY381 4.5 15.1 1.0 OD1 C:ASP216 4.6 14.7 1.0 CG A:GLN65 4.7 14.2 1.0 C A:PRO383 4.7 15.0 1.0 CA A:HIS382 4.7 14.1 1.0 N A:SER384 4.7 14.5 1.0 CA A:GLY381 4.7 14.4 1.0 CG2 A:THR380 4.8 14.2 1.0 OE1 A:GLN91 4.8 17.5 1.0 O C:ASP216 5.0 14.9 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07


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 S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with F2X-Entry Library Fragment B07 within 5.0Å range: probe atom residue distance (Å) B Occ C:K502 b:14.4 occ:1.00 O C:HIS382 2.7 15.1 1.0 O C:THR380 2.7 15.2 1.0 O C:HOH809 2.8 14.9 1.0 OG1 C:THR380 2.8 15.2 1.0 O C:HOH816 2.9 15.2 1.0 O A:HOH790 3.1 14.8 1.0 OE1 C:GLN65 3.2 14.7 1.0 NE2 C:GLN65 3.4 14.1 1.0 CD C:GLN65 3.4 12.0 1.0 CB C:THR380 3.5 13.3 1.0 C C:HIS382 3.6 13.3 1.0 C C:THR380 3.6 15.6 1.0 O C:GLY381 3.8 15.3 1.0 CA C:PRO383 4.0 12.7 1.0 N6 C:ADE512 4.0 14.4 1.0 C C:GLY381 4.1 12.6 1.0 N C:PRO383 4.2 13.1 1.0 CA C:THR380 4.2 14.4 1.0 CB A:ASP216 4.3 15.1 1.0 O C:HOH953 4.4 17.3 1.0 N C:HIS382 4.4 14.3 1.0 CG A:ASP216 4.5 15.5 1.0 N C:GLY381 4.5 13.7 1.0 OD1 A:ASP216 4.6 15.2 1.0 CG C:GLN65 4.6 14.4 1.0 CA C:HIS382 4.6 13.7 1.0 C C:PRO383 4.7 13.6 1.0 CA C:GLY381 4.7 13.8 1.0 N C:SER384 4.7 13.1 1.0 CG2 C:THR380 4.7 13.8 1.0 OE1 C:GLN91 4.8 17.1 1.0 O A:ASP216 5.0 14.1 1.0

P.H.Malecki, M.Gawel, M.Stepniewska, K.Brzezinski. Crystal Structure of S-Adenosyl-L-Homocysteine Hydrolase From P. Aeruginosa in Complex with Fragment F2X-Entry B07 To Be Published.