Sodium in PDB 5ksg: Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid

All present enzymatic activity of Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid:
1.11.1.21;

The structure of Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid, PDB code: 5ksg was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	96.54 / 1.62
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.665, 115.928, 174.349, 90.00, 90.00, 90.00
R / Rfree (%)	13.5 / 15.9

The structure of Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid also contains other interesting chemical elements:

Iron	(Fe)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Sodium atom in the Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid (pdb code 5ksg). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid, PDB code: 5ksg:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid within 5.0Å range: probe atom residue distance (Å) B Occ A:Na802 b:14.5 occ:1.00 O A:GLY124 2.3 13.5 1.0 O A:HOH1532 2.3 18.8 1.0 O A:HOH968 2.4 17.5 1.0 O A:SER494 2.4 15.0 1.0 O A:GLY122 2.4 13.6 1.0 C A:SER494 3.2 15.0 1.0 C A:GLY124 3.4 14.1 1.0 C A:GLY122 3.5 12.8 1.0 N A:GLY124 3.6 13.1 1.0 C A:ARG123 3.6 12.5 1.0 CA A:ARG123 3.6 12.5 1.0 O A:HOH1595 3.9 18.9 1.0 CA A:SER494 3.9 13.3 1.0 OD2 A:ASP427 4.0 15.3 1.0 N A:ARG123 4.0 13.1 1.0 O A:HOH1072 4.0 30.5 1.0 N A:ASP495 4.1 13.2 1.0 CA A:GLY124 4.1 13.6 1.0 CB A:ASP427 4.2 15.4 1.0 CB A:SER494 4.2 14.2 1.0 O A:ARG123 4.2 13.5 1.0 CA A:ASP495 4.4 13.4 1.0 N A:GLY125 4.5 12.0 1.0 CL A:CL803 4.6 29.3 1.0 CG A:ASP427 4.6 17.2 1.0 CB A:ASP495 4.6 13.3 1.0 CD1 A:TYR117 4.7 13.9 1.0 OE2 A:GLU128 4.7 28.6 1.0 CA A:GLY122 4.8 13.4 1.0 CA A:GLY125 4.9 12.9 1.0 CB A:ARG123 4.9 14.7 1.0 OG A:SER494 5.0 13.3 1.0 CE1 A:TYR117 5.0 13.2 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the W153F Variant of Catalase-Peroxidase From B. Pseudomallei Treated with Isoniazid within 5.0Å range: probe atom residue distance (Å) B Occ B:Na802 b:14.9 occ:1.00 O B:HOH1529 2.3 18.7 1.0 O B:GLY124 2.3 13.7 1.0 O B:GLY122 2.4 12.1 1.0 O B:SER494 2.4 14.3 1.0 O B:HOH987 2.4 16.9 1.0 C B:SER494 3.3 15.2 1.0 C B:GLY124 3.5 13.9 1.0 C B:GLY122 3.5 12.1 1.0 N B:GLY124 3.6 13.8 1.0 C B:ARG123 3.6 12.8 1.0 CA B:ARG123 3.6 12.7 1.0 CA B:SER494 3.9 13.4 1.0 O B:HOH1600 3.9 17.2 1.0 OD2 B:ASP427 4.0 17.4 1.0 N B:ARG123 4.0 12.9 1.0 O B:HOH1218 4.1 28.4 1.0 CB B:SER494 4.1 12.9 1.0 CA B:GLY124 4.1 12.9 1.0 N B:ASP495 4.2 13.0 1.0 O B:ARG123 4.2 12.4 1.0 CB B:ASP427 4.2 17.0 1.0 CA B:ASP495 4.5 13.1 1.0 CL B:CL803 4.6 26.4 1.0 N B:GLY125 4.6 11.3 1.0 CB B:ASP495 4.6 13.4 1.0 OE2 B:GLU128 4.7 27.8 1.0 CD1 B:TYR117 4.7 13.1 1.0 CG B:ASP427 4.7 17.6 1.0 CA B:GLY122 4.8 12.5 1.0 CA B:GLY125 4.9 12.8 1.0 CB B:ARG123 4.9 13.2 1.0 OG B:SER494 4.9 14.0 1.0 CE1 B:TYR117 5.0 12.5 1.0

P.C.Loewen, P.C.Loewen. N/A N/A.