Sodium in PDB 4jex: Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline

All present enzymatic activity of Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline:
2.6.1.11; 2.6.1.17;

The structure of Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline, PDB code: 4jex 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)	25.01 / 1.43
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.990, 112.780, 65.340, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 17.6

The binding sites of Sodium atom in the Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline (pdb code 4jex). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline, PDB code: 4jex:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Y21K 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 Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline within 5.0Å range: probe atom residue distance (Å) B Occ A:Na512 b:11.1 occ:1.00 O A:HOH917 2.3 23.9 1.0 O A:HOH705 2.3 20.6 1.0 O A:ILE94 2.3 10.4 1.0 O A:ALA99 2.3 8.8 1.0 O A:THR97 2.4 8.8 1.0 C A:ILE94 3.4 10.1 1.0 C A:ALA99 3.5 8.6 1.0 C A:THR97 3.5 8.5 1.0 C A:PHE98 3.6 8.8 1.0 N A:ALA99 3.7 8.8 1.0 O A:PHE98 3.8 9.7 1.0 CG2 A:ILE94 3.9 9.9 1.0 CA A:ILE94 4.0 9.7 1.0 CA A:PHE98 4.1 8.5 1.0 CA A:ALA99 4.1 8.7 1.0 N A:PHE98 4.2 8.5 1.0 N A:THR97 4.5 8.5 1.0 N A:GLU100 4.5 8.4 1.0 N A:ASP95 4.5 10.2 1.0 O A:HOH833 4.5 26.2 1.0 O A:HOH726 4.5 25.6 1.0 CB A:ILE94 4.6 9.9 1.0 CA A:THR97 4.6 8.4 1.0 OG1 A:THR97 4.7 8.4 1.0 O A:HOH874 4.8 29.4 1.0 CA A:ASP95 4.8 10.8 1.0 C A:ASP95 4.9 10.2 1.0 CA A:GLU100 4.9 8.9 1.0 CB A:ALA99 5.0 9.0 1.0 O A:ASP95 5.0 10.9 1.0

Sodium binding site 2 out of 2 in the Y21K 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 Y21K Mutant of N-Acetylornithine Aminotransferase Complexed with L- Canaline within 5.0Å range: probe atom residue distance (Å) B Occ B:Na511 b:11.1 occ:1.00 O B:HOH726 2.3 22.5 1.0 O B:ILE94 2.3 10.7 1.0 O B:HOH716 2.4 21.2 1.0 O B:THR97 2.4 9.1 1.0 O B:ALA99 2.4 10.3 1.0 O B:HOH914 2.6 26.8 1.0 C B:ILE94 3.4 10.3 1.0 C B:ALA99 3.5 9.5 1.0 C B:THR97 3.6 8.8 1.0 C B:PHE98 3.6 9.0 1.0 N B:ALA99 3.7 9.2 1.0 O B:PHE98 3.8 10.1 1.0 CG2 B:ILE94 4.0 10.1 1.0 CA B:ILE94 4.1 10.0 1.0 CA B:PHE98 4.1 8.8 1.0 CA B:ALA99 4.2 9.3 1.0 O B:HOH864 4.2 35.6 1.0 N B:PHE98 4.3 8.7 1.0 O B:HOH802 4.5 25.2 1.0 N B:THR97 4.5 8.8 1.0 N B:ASP95 4.5 10.2 1.0 O B:HOH842 4.5 24.7 1.0 N B:GLU100 4.6 9.7 1.0 CA B:THR97 4.6 8.5 1.0 CB B:ILE94 4.6 10.1 1.0 O B:HOH761 4.7 29.4 1.0 CA B:ASP95 4.7 10.8 1.0 OG1 B:THR97 4.8 8.1 1.0 O B:HOH913 4.8 39.9 1.0 C B:ASP95 4.8 10.4 1.0 CA B:GLU100 4.9 9.8 1.0 O B:ASP95 4.9 10.8 1.0 O B:HOH898 4.9 33.5 1.0 CB B:ALA99 5.0 9.9 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.