Sodium in PDB 4jey: E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium

All present enzymatic activity of E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium:
2.6.1.11; 2.6.1.17;

The structure of E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium, PDB code: 4jey was solved by S.Bisht, S.R.Bharath, M.R.N.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.00 / 1.55
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.790, 111.860, 65.230, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 18.3

The binding sites of Sodium atom in the E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium (pdb code 4jey). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium, PDB code: 4jey:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium within 5.0Å range: probe atom residue distance (Å) B Occ A:Na508 b:16.0 occ:1.00 O A:HOH824 2.3 31.3 1.0 O A:HOH801 2.3 32.7 1.0 O A:ALA99 2.4 9.6 1.0 O A:ILE94 2.4 11.0 1.0 O A:THR97 2.5 10.3 1.0 O A:HOH951 3.1 36.2 1.0 C A:ILE94 3.5 11.0 1.0 C A:ALA99 3.5 9.6 1.0 C A:PHE98 3.6 9.7 1.0 C A:THR97 3.7 10.0 1.0 O A:PHE98 3.7 10.3 1.0 N A:ALA99 3.8 9.5 1.0 CG2 A:ILE94 3.9 11.6 1.0 CA A:ILE94 4.1 10.7 1.0 CA A:PHE98 4.1 9.4 1.0 CA A:ALA99 4.3 9.6 1.0 N A:PHE98 4.3 9.8 1.0 O A:HOH854 4.4 37.9 1.0 O A:HOH924 4.5 31.3 1.0 O A:HOH887 4.5 32.0 1.0 N A:GLU100 4.5 9.7 1.0 N A:ASP95 4.6 10.8 1.0 N A:THR97 4.6 10.2 1.0 CB A:ILE94 4.6 10.8 1.0 CA A:THR97 4.8 9.8 1.0 CA A:ASP95 4.9 11.7 1.0 CA A:GLU100 4.9 10.0 1.0 OG1 A:THR97 4.9 9.6 1.0 CG A:GLU100 4.9 11.1 1.0 C A:ASP95 5.0 11.5 1.0

Sodium binding site 2 out of 2 in the E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of E198A Mutant of N-Acetylornithine Aminotransferase From Salmonella Typhimurium within 5.0Å range: probe atom residue distance (Å) B Occ B:Na505 b:16.6 occ:1.00 O B:HOH745 2.3 27.4 1.0 O B:HOH847 2.4 37.9 1.0 O B:ILE94 2.4 11.9 1.0 O B:ALA99 2.5 10.9 1.0 O B:THR97 2.5 11.0 1.0 C B:ILE94 3.5 11.4 1.0 C B:ALA99 3.6 10.8 1.0 C B:THR97 3.7 10.4 1.0 C B:PHE98 3.7 10.7 1.0 N B:ALA99 3.8 10.9 1.0 O B:PHE98 3.8 11.6 1.0 CG2 B:ILE94 3.9 11.5 1.0 CA B:ILE94 4.1 10.9 1.0 CA B:PHE98 4.2 10.4 1.0 O B:HOH786 4.3 31.8 1.0 CA B:ALA99 4.3 10.7 1.0 N B:PHE98 4.4 10.6 1.0 N B:ASP95 4.6 11.2 1.0 N B:GLU100 4.6 10.6 1.0 N B:THR97 4.6 10.0 1.0 CB B:ILE94 4.6 11.1 1.0 CA B:THR97 4.7 9.9 1.0 CA B:ASP95 4.8 12.5 1.0 CA B:GLU100 4.9 10.9 1.0 C B:ASP95 4.9 11.7 1.0 CG B:GLU100 4.9 12.4 1.0 OG1 B:THR97 4.9 9.1 1.0 O B:ASP95 4.9 12.9 1.0

S.Bisht, S.R.Bharath, M.R.N.Murthy. Conformational Transitions, Ligand Specificity and Catalysis in N-Acetylornithine Aminotransferase: Implications on Drug Designing and Rational Enzyme Engineering in Omega Aminotransferases To Be Published.