Sodium in PDB 6cfq: Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound

All present enzymatic activity of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound:
1.11.1.21;

The structure of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound, PDB code: 6cfq 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)	96.32 / 1.72
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.641, 115.506, 174.546, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 17

The structure of Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound 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 D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound (pdb code 6cfq). 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 D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound, PDB code: 6cfq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound


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 D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Na802 b:17.6 occ:1.00 O A:GLY124 2.3 17.4 1.0 O A:SER494 2.3 17.4 1.0 O A:GLY122 2.4 16.1 1.0 O A:HOH1011 2.4 18.9 1.0 O A:HOH1495 2.4 20.1 1.0 C A:SER494 3.2 17.8 1.0 C A:GLY124 3.5 16.7 1.0 C A:GLY122 3.5 15.6 1.0 N A:GLY124 3.6 16.8 1.0 C A:ARG123 3.6 16.4 1.0 CA A:ARG123 3.6 15.7 1.0 O A:HOH1555 3.9 22.1 1.0 CA A:SER494 3.9 16.8 1.0 OD2 A:ASP427 4.0 17.9 1.0 N A:ARG123 4.1 15.2 1.0 N A:ASP495 4.1 15.5 1.0 O A:HOH1038 4.1 32.5 1.0 CB A:ASP427 4.1 17.4 1.0 CA A:GLY124 4.2 16.6 1.0 CB A:SER494 4.2 17.6 1.0 O A:ARG123 4.2 15.5 1.0 CA A:ASP495 4.4 17.5 1.0 CB A:ASP495 4.6 18.2 1.0 N A:GLY125 4.6 14.6 1.0 CG A:ASP427 4.6 19.0 1.0 CL A:CL803 4.6 34.3 1.0 CD1 A:TYR117 4.7 16.6 1.0 OE2 A:GLU128 4.8 28.2 1.0 CA A:GLY122 4.8 16.2 1.0 CA A:GLY125 4.9 15.3 1.0 CB A:ARG123 4.9 17.4 1.0 CE1 A:TYR117 4.9 16.1 1.0 OG A:SER494 5.0 17.6 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound


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 D141N Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Na802 b:17.6 occ:1.00 O B:HOH1486 2.3 21.6 1.0 O B:GLY124 2.3 17.0 1.0 O B:GLY122 2.3 15.5 1.0 O B:SER494 2.4 17.0 1.0 O B:HOH1088 2.4 20.9 1.0 C B:SER494 3.2 16.8 1.0 C B:GLY124 3.5 16.8 1.0 C B:GLY122 3.5 15.7 1.0 N B:GLY124 3.6 16.5 1.0 C B:ARG123 3.6 16.3 1.0 CA B:ARG123 3.6 15.1 1.0 O B:HOH1549 3.9 20.3 1.0 CA B:SER494 3.9 16.9 1.0 OD2 B:ASP427 4.0 17.6 1.0 N B:ARG123 4.0 14.9 1.0 CB B:SER494 4.1 16.7 1.0 N B:ASP495 4.1 16.0 1.0 O B:ARG123 4.1 15.0 1.0 CA B:GLY124 4.2 15.5 1.0 CB B:ASP427 4.2 19.2 1.0 O B:HOH1117 4.2 28.3 1.0 CA B:ASP495 4.4 16.5 1.0 CB B:ASP495 4.6 15.7 1.0 N B:GLY125 4.6 15.1 1.0 CL B:CL803 4.6 30.2 1.0 CG B:ASP427 4.7 19.0 1.0 OE2 B:GLU128 4.7 28.1 1.0 CD1 B:TYR117 4.7 16.1 1.0 CA B:GLY122 4.8 15.9 1.0 CA B:GLY125 4.9 15.9 1.0 CB B:ARG123 4.9 16.4 1.0 CE1 B:TYR117 4.9 16.7 1.0 OG B:SER494 5.0 17.0 1.0

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