Sodium in PDB 4jf0: N79R Mutant of N-Acetylornithine Aminotransferase

All present enzymatic activity of N79R Mutant of N-Acetylornithine Aminotransferase:
2.6.1.11; 2.6.1.17;

The structure of N79R Mutant of N-Acetylornithine Aminotransferase, PDB code: 4jf0 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)	50.00 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.914, 113.604, 69.183, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20.2

The binding sites of Sodium atom in the N79R Mutant of N-Acetylornithine Aminotransferase (pdb code 4jf0). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the N79R Mutant of N-Acetylornithine Aminotransferase, PDB code: 4jf0:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the N79R Mutant of N-Acetylornithine Aminotransferase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of N79R Mutant of N-Acetylornithine Aminotransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Na504 b:33.6 occ:1.00 O A:HOH609 2.3 43.4 1.0 O A:ILE94 2.3 30.7 1.0 O A:THR97 2.4 27.4 1.0 O A:HOH658 2.4 46.9 1.0 O A:ALA99 2.5 28.8 1.0 C A:ILE94 3.4 30.3 1.0 C A:THR97 3.5 27.9 1.0 C A:ALA99 3.6 28.1 1.0 C A:PHE98 3.6 28.5 1.0 O A:PHE98 3.8 28.9 1.0 N A:ALA99 3.8 28.2 1.0 CG2 A:ILE94 4.0 30.0 1.0 CA A:ILE94 4.1 29.6 1.0 CA A:PHE98 4.1 27.9 1.0 N A:PHE98 4.3 27.8 1.0 CA A:ALA99 4.3 28.6 1.0 N A:ASP95 4.5 31.2 1.0 N A:THR97 4.5 27.8 1.0 CA A:THR97 4.6 27.5 1.0 N A:GLU100 4.6 27.4 1.0 CB A:ILE94 4.7 29.6 1.0 O A:HOH736 4.7 53.5 1.0 CA A:ASP95 4.8 31.4 1.0 OG1 A:THR97 4.8 26.4 1.0 C A:ASP95 4.8 30.4 1.0 O A:ASP95 4.9 30.3 1.0 CA A:GLU100 5.0 28.9 1.0

Sodium binding site 2 out of 2 in the N79R Mutant of N-Acetylornithine Aminotransferase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of N79R Mutant of N-Acetylornithine Aminotransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Na502 b:32.8 occ:1.00 O B:ILE94 2.3 29.4 1.0 O B:HOH606 2.4 37.3 1.0 O B:THR97 2.4 27.8 1.0 O B:ALA99 2.4 28.9 1.0 O B:HOH601 2.4 40.3 1.0 C B:ILE94 3.5 30.0 1.0 C B:THR97 3.5 28.3 1.0 C B:ALA99 3.5 29.3 1.0 C B:PHE98 3.6 29.0 1.0 N B:ALA99 3.7 28.6 1.0 O B:PHE98 3.8 29.8 1.0 CG2 B:ILE94 4.0 30.2 1.0 CA B:ILE94 4.1 29.1 1.0 CA B:PHE98 4.1 28.5 1.0 CA B:ALA99 4.2 28.9 1.0 N B:PHE98 4.2 28.5 1.0 O B:HOH751 4.3 50.7 1.0 N B:THR97 4.5 28.6 1.0 N B:ASP95 4.5 30.3 1.0 N B:GLU100 4.6 28.9 1.0 CA B:THR97 4.6 28.7 1.0 CB B:ILE94 4.6 30.1 1.0 OG1 B:THR97 4.8 29.3 1.0 CA B:ASP95 4.8 31.2 1.0 CA B:GLU100 4.9 29.7 1.0 C B:ASP95 4.9 30.8 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.