Potassium in PDB 2bty: Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine

All present enzymatic activity of Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine:
2.7.2.8;

The structure of Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine, PDB code: 2bty was solved by F.Gil-Ortiz, M.L.Fernandez-Murga, I.Fita, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 2.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	94.998, 207.709, 117.996, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 27.3

The binding sites of Potassium atom in the Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine (pdb code 2bty). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine, PDB code: 2bty:

Potassium binding site 1 out of 1 in the Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Acetylglutamate Kinase From Thermotoga Maritima Complexed with Its Inhibitor Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:K1285 b:78.4 occ:1.00 OD2 A:ASP160 2.9 42.4 1.0 OD1 A:ASP160 3.6 42.9 1.0 CG A:ASP160 3.6 40.9 1.0 CE A:LYS50 3.8 36.1 1.0 CG A:LYS50 4.4 35.8 1.0 CD A:LYS50 4.5 36.1 1.0 NZ C:LYS17 4.5 55.2 1.0 NZ A:LYS50 4.8 36.6 1.0 CE1 A:TYR51 5.0 45.2 1.0

S.Ramon-Maiques, M.L.Fernandez-Murga, F.Gil-Ortiz, A.Vagin, I.Fita, V.Rubio. Structural Bases of Feed-Back Control of Arginine Biosynthesis, Revealed By the Structure of Two Hexameric N-Acetylglutamate Kinases, From Thermotoga Maritima and Pseudomonas Aeruginosa J.Mol.Biol. V. 356 695 2006.
ISSN: ISSN 0022-2836
PubMed: 16376937
DOI: 10.1016/J.JMB.2005.11.079