Sodium in PDB 3fvs: Human Kynurenine Aminotransferase I in Complex with Glycerol

All present enzymatic activity of Human Kynurenine Aminotransferase I in Complex with Glycerol:
2.6.1.64; 2.6.1.7; 4.4.1.13;

The structure of Human Kynurenine Aminotransferase I in Complex with Glycerol, PDB code: 3fvs was solved by Q.Han, H.Robinson, T.Cai, D.A.Tagle, J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.55 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.707, 107.219, 81.597, 90.00, 112.78, 90.00
R / Rfree (%)	17.4 / 19.5

The binding sites of Sodium atom in the Human Kynurenine Aminotransferase I in Complex with Glycerol (pdb code 3fvs). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Human Kynurenine Aminotransferase I in Complex with Glycerol, PDB code: 3fvs:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Human Kynurenine Aminotransferase I in Complex with Glycerol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Kynurenine Aminotransferase I in Complex with Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ A:Na423 b:24.6 occ:1.00 O A:HOH494 2.3 23.4 1.0 O A:HIS206 2.3 15.8 1.0 O A:HOH664 2.4 27.1 1.0 O A:HOH680 2.4 29.3 1.0 O A:HOH558 2.4 34.7 1.0 O A:HOH688 2.8 37.8 1.0 C A:HIS206 3.4 16.2 1.0 CA A:HIS206 4.2 16.3 1.0 O A:HOH443 4.2 44.7 1.0 O A:SER173 4.2 17.1 1.0 O A:ASP207 4.3 16.3 1.0 CB A:ASP207 4.4 16.7 1.0 CB A:HIS206 4.4 16.7 1.0 CA A:SER173 4.5 17.4 1.0 N A:ASP207 4.5 15.6 1.0 O A:THR172 4.5 16.8 1.0 C A:SER173 4.7 16.4 1.0 C A:ASP207 4.7 15.9 1.0 CA A:ASP207 4.7 16.0 1.0 O A:THR175 4.8 13.7 1.0

Sodium binding site 2 out of 2 in the Human Kynurenine Aminotransferase I in Complex with Glycerol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Human Kynurenine Aminotransferase I in Complex with Glycerol within 5.0Å range: probe atom residue distance (Å) B Occ B:Na424 b:21.8 occ:1.00 O B:HOH685 2.2 21.1 1.0 O B:HOH687 2.3 29.3 1.0 O B:HIS206 2.4 17.0 1.0 O B:HOH689 2.5 28.4 1.0 O B:HOH686 2.5 25.4 1.0 O B:HOH471 2.5 24.6 1.0 C B:HIS206 3.6 16.8 1.0 O B:SER173 4.2 18.5 1.0 CA B:HIS206 4.2 17.2 1.0 CA B:SER173 4.4 18.9 1.0 O B:ASP207 4.4 17.1 1.0 CB B:HIS206 4.4 17.5 1.0 O B:THR172 4.4 18.5 1.0 CB B:ASP207 4.6 17.1 1.0 C B:SER173 4.6 18.4 1.0 N B:ASP207 4.6 16.4 1.0 O B:THR175 4.6 16.0 1.0 O B:HOH676 4.6 27.0 1.0 C B:ASP207 4.8 16.4 1.0 CA B:ASP207 4.9 16.9 1.0

Q.Han, H.Robinson, T.Cai, D.A.Tagle, J.Li. Structural Insight Into the Inhibition of Human Kynurenine Aminotransferase I/Glutamine Transaminase K J.Med.Chem. V. 52 2786 2009.
ISSN: ISSN 0022-2623
PubMed: 19338303
DOI: 10.1021/JM9000874