Sodium in PDB 4jev: N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine

All present enzymatic activity of N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine:
2.6.1.11; 2.6.1.17;

The structure of N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine, PDB code: 4jev 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)	36.69 / 1.67
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.660, 111.860, 65.170, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 18.8

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

Sodium binding site 1 out of 2 in the N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine within 5.0Å range: probe atom residue distance (Å) B Occ A:Na503 b:12.7 occ:1.00 O A:HOH794 2.3 27.4 1.0 O A:ILE94 2.3 11.8 1.0 O A:HOH837 2.4 25.6 1.0 O A:ALA99 2.4 10.0 1.0 O A:THR97 2.5 10.1 1.0 O A:HOH951 2.5 25.9 1.0 C A:ILE94 3.4 11.6 1.0 C A:ALA99 3.6 10.3 1.0 C A:THR97 3.6 10.1 1.0 C A:PHE98 3.7 10.1 1.0 O A:PHE98 3.8 10.3 1.0 N A:ALA99 3.8 10.2 1.0 CG2 A:ILE94 4.0 11.2 1.0 CA A:ILE94 4.0 11.2 1.0 CA A:PHE98 4.2 10.3 1.0 O A:HOH782 4.2 29.3 1.0 CA A:ALA99 4.3 10.1 1.0 O A:HOH797 4.3 38.5 1.0 N A:PHE98 4.3 10.0 1.0 O A:HOH729 4.4 30.6 1.0 N A:ASP95 4.5 12.2 1.0 N A:THR97 4.5 10.3 1.0 N A:GLU100 4.6 10.1 1.0 O A:HOH906 4.6 35.6 1.0 CB A:ILE94 4.6 11.1 1.0 CA A:THR97 4.7 10.0 1.0 CA A:ASP95 4.8 13.2 1.0 C A:ASP95 4.8 12.3 1.0 CA A:GLU100 4.9 10.3 1.0 CG A:GLU100 4.9 11.8 1.0 O A:ASP95 4.9 12.3 1.0 O B:HOH796 4.9 24.6 1.0 OG1 A:THR97 4.9 10.1 1.0

Sodium binding site 2 out of 2 in the N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of N-Acetylornithine Aminotransferase From S. Typhimurium Complexed with Gabaculine within 5.0Å range: probe atom residue distance (Å) B Occ B:Na503 b:14.7 occ:1.00 O B:HOH931 2.3 25.0 1.0 O B:HOH603 2.4 21.3 1.0 O B:ILE94 2.4 12.8 1.0 O B:THR97 2.4 10.9 1.0 O B:ALA99 2.4 11.1 1.0 C B:ILE94 3.5 12.2 1.0 C B:THR97 3.5 10.7 1.0 C B:ALA99 3.6 11.6 1.0 C B:PHE98 3.6 11.4 1.0 N B:ALA99 3.7 10.9 1.0 O B:PHE98 3.8 11.9 1.0 CG2 B:ILE94 3.9 12.5 1.0 CA B:ILE94 4.1 12.0 1.0 CA B:PHE98 4.1 11.0 1.0 CA B:ALA99 4.2 11.3 1.0 N B:PHE98 4.3 10.7 1.0 O B:HOH883 4.5 32.2 1.0 N B:THR97 4.5 10.5 1.0 N B:ASP95 4.6 12.5 1.0 N B:GLU100 4.6 11.8 1.0 CB B:ILE94 4.6 12.2 1.0 CA B:THR97 4.7 10.5 1.0 O A:HOH915 4.7 28.9 1.0 CA B:ASP95 4.8 13.2 1.0 OG1 B:THR97 4.8 10.7 1.0 C B:ASP95 4.9 13.1 1.0 CG B:GLU100 4.9 13.7 1.0 CA B:GLU100 4.9 12.1 1.0 O B:ASP95 4.9 13.3 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.