Sodium in PDB 6cdq: Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.

All present enzymatic activity of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound.:
1.11.1.21;

The structure of Crystal Structure of the W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound., PDB code: 6cdq 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)	174.10 / 1.92
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.531, 114.896, 174.099, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 19.9

The structure of Crystal Structure of the W202F 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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. (pdb code 6cdq). 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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound., PDB code: 6cdq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the W202F 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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. within 5.0Å range: probe atom residue distance (Å) B Occ A:Na802 b:20.5 occ:1.00 O A:GLY124 2.3 19.3 1.0 O A:SER494 2.3 19.3 1.0 O A:GLY122 2.3 18.9 1.0 O A:HOH1180 2.4 20.9 1.0 O A:HOH1412 2.5 27.2 1.0 C A:SER494 3.2 19.1 1.0 C A:GLY124 3.4 20.9 1.0 C A:GLY122 3.5 17.3 1.0 C A:ARG123 3.6 20.4 1.0 CA A:ARG123 3.6 18.7 1.0 N A:GLY124 3.6 21.0 1.0 CA A:SER494 3.9 18.4 1.0 O A:HOH1136 4.0 30.4 1.0 OD2 A:ASP427 4.0 20.1 1.0 N A:ARG123 4.0 19.1 1.0 O A:HOH1447 4.1 17.3 1.0 N A:ASP495 4.1 20.1 1.0 CB A:ASP427 4.1 21.7 1.0 CA A:GLY124 4.1 22.1 1.0 CB A:SER494 4.2 18.8 1.0 O A:ARG123 4.2 17.8 1.0 CA A:ASP495 4.4 18.4 1.0 CB A:ASP495 4.5 19.5 1.0 N A:GLY125 4.6 19.2 1.0 CG A:ASP427 4.6 23.0 1.0 CD1 A:TYR117 4.7 20.3 1.0 CL A:CL803 4.7 30.8 1.0 CA A:GLY122 4.8 18.5 1.0 OE2 A:GLU128 4.8 33.0 1.0 CA A:GLY125 4.9 19.3 1.0 CB A:ARG123 4.9 20.4 1.0 OG A:SER494 4.9 19.3 1.0 CE1 A:TYR117 4.9 18.9 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the W202F 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 W202F Variant of Catalase-Peroxidase From B. Pseudomallei with Inh Bound. within 5.0Å range: probe atom residue distance (Å) B Occ B:Na802 b:19.3 occ:1.00 O B:GLY124 2.3 17.8 1.0 O B:SER494 2.3 17.1 1.0 O B:GLY122 2.3 18.4 1.0 O B:HOH1187 2.4 24.2 1.0 O B:HOH1355 2.4 24.1 1.0 C B:SER494 3.2 19.1 1.0 C B:GLY124 3.5 18.5 1.0 C B:GLY122 3.5 18.4 1.0 C B:ARG123 3.7 21.4 1.0 CA B:ARG123 3.7 19.5 1.0 N B:GLY124 3.7 20.9 1.0 CA B:SER494 3.9 19.0 1.0 O B:HOH1437 4.0 22.6 1.0 OD2 B:ASP427 4.0 21.4 1.0 N B:ASP495 4.0 19.0 1.0 N B:ARG123 4.1 17.9 1.0 O B:HOH953 4.1 29.4 1.0 CB B:SER494 4.1 16.6 1.0 CB B:ASP427 4.1 22.4 1.0 CA B:GLY124 4.2 19.9 1.0 O B:ARG123 4.2 19.2 1.0 CA B:ASP495 4.4 17.4 1.0 OE2 B:GLU128 4.5 32.8 1.0 CB B:ASP495 4.5 17.1 1.0 N B:GLY125 4.6 18.4 1.0 CG B:ASP427 4.6 19.8 1.0 CD1 B:TYR117 4.7 19.2 1.0 CL B:CL803 4.7 27.5 1.0 CA B:GLY122 4.8 19.1 1.0 OG B:SER494 4.9 15.9 1.0 CA B:GLY125 4.9 18.5 1.0 CE1 B:TYR117 4.9 19.3 1.0 CB B:ARG123 4.9 18.1 1.0

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