Sodium in PDB 4jez: N79R Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline

All present enzymatic activity of N79R Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline:
2.6.1.11; 2.6.1.17;

The structure of N79R Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline, PDB code: 4jez 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)	28.01 / 1.55
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.600, 112.030, 65.110, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 17.6

The binding sites of Sodium atom in the N79R Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline (pdb code 4jez). 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 Complexed with L- Canaline, PDB code: 4jez:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the N79R Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline


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 Complexed with L- Canaline within 5.0Å range: probe atom residue distance (Å) B Occ A:Na509 b:13.8 occ:1.00 O A:HOH745 2.2 25.2 1.0 O A:HOH724 2.3 23.8 1.0 O A:ILE94 2.3 12.5 1.0 O A:ALA99 2.4 10.9 1.0 O A:THR97 2.4 11.2 1.0 O A:HOH860 2.8 37.2 1.0 C A:ILE94 3.4 12.2 1.0 C A:ALA99 3.5 10.8 1.0 C A:THR97 3.6 11.0 1.0 C A:PHE98 3.6 10.9 1.0 N A:ALA99 3.7 10.8 1.0 O A:PHE98 3.8 12.0 1.0 CG2 A:ILE94 3.9 12.4 1.0 CA A:ILE94 4.1 11.9 1.0 CA A:PHE98 4.1 10.8 1.0 CA A:ALA99 4.2 10.9 1.0 N A:PHE98 4.3 10.9 1.0 O A:HOH778 4.5 33.2 1.0 N A:ASP95 4.5 12.6 1.0 N A:THR97 4.5 11.4 1.0 O A:HOH836 4.5 34.2 1.0 N A:GLU100 4.6 10.4 1.0 CB A:ILE94 4.6 12.4 1.0 CA A:THR97 4.7 11.1 1.0 CA A:ASP95 4.7 13.6 1.0 OG1 A:THR97 4.8 11.1 1.0 C A:ASP95 4.8 13.1 1.0 CA A:GLU100 4.9 10.8 1.0 O A:ASP95 5.0 14.1 1.0

Sodium binding site 2 out of 2 in the N79R Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline


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 Complexed with L- Canaline within 5.0Å range: probe atom residue distance (Å) B Occ B:Na508 b:14.8 occ:1.00 O B:HOH736 2.2 29.0 1.0 O B:HOH771 2.3 27.5 1.0 O B:ILE94 2.4 13.6 1.0 O B:THR97 2.4 11.4 1.0 O B:ALA99 2.4 11.7 1.0 C B:ILE94 3.4 13.0 1.0 C B:ALA99 3.5 12.0 1.0 C B:THR97 3.6 11.1 1.0 C B:PHE98 3.6 11.6 1.0 N B:ALA99 3.7 11.4 1.0 O B:PHE98 3.8 12.2 1.0 CG2 B:ILE94 3.9 13.1 1.0 CA B:ILE94 4.1 12.4 1.0 CA B:PHE98 4.1 11.2 1.0 CA B:ALA99 4.2 12.0 1.0 N B:PHE98 4.3 11.4 1.0 O B:HOH763 4.4 32.9 1.0 N B:ASP95 4.5 12.9 1.0 N B:THR97 4.6 11.0 1.0 O B:HOH845 4.6 36.6 1.0 N B:GLU100 4.6 11.7 1.0 CB B:ILE94 4.6 12.8 1.0 CA B:THR97 4.7 10.7 1.0 CA B:ASP95 4.8 14.0 1.0 OG1 B:THR97 4.8 10.1 1.0 C B:ASP95 4.9 13.5 1.0 CA B:GLU100 4.9 12.4 1.0 CG B:GLU100 5.0 14.7 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.