Sodium in PDB 5sxw: Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei

All present enzymatic activity of Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei:
1.11.1.21;

The structure of Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei, PDB code: 5sxw 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)	20.00 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.340, 116.020, 174.710, 90.00, 90.00, 90.00
R / Rfree (%)	14.3 / 16.9

The structure of Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei (pdb code 5sxw). 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 E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei, PDB code: 5sxw:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei


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 E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ A:Na802 b:18.1 occ:1.00 O A:GLY124 2.4 13.7 1.0 O A:HOH1031 2.4 18.6 1.0 O A:GLY122 2.5 13.0 1.0 O A:SER494 2.5 19.1 1.0 O A:HOH1608 2.8 18.6 1.0 C A:SER494 3.3 14.9 1.0 N A:GLY124 3.4 12.9 1.0 C A:GLY124 3.5 13.5 1.0 C A:ARG123 3.5 13.1 1.0 CA A:ARG123 3.5 13.5 1.0 C A:GLY122 3.6 13.7 1.0 O A:HOH934 3.9 27.4 1.0 O A:HOH1637 3.9 19.3 1.0 CA A:SER494 3.9 12.2 1.0 N A:ARG123 4.0 13.2 1.0 O A:HOH1415 4.1 35.7 1.0 CA A:GLY124 4.1 13.7 1.0 CB A:SER494 4.1 13.1 1.0 N A:ASP495 4.1 13.5 1.0 OD2 A:ASP427 4.1 15.6 1.0 O A:ARG123 4.2 13.7 1.0 CB A:ASP427 4.2 16.3 1.0 CA A:ASP495 4.4 13.2 1.0 N A:GLY125 4.6 12.5 1.0 CB A:ASP495 4.6 12.8 1.0 CD1 A:TYR117 4.7 13.2 1.0 CB A:ARG123 4.8 16.0 1.0 CG A:ASP427 4.8 18.4 1.0 CA A:GLY122 4.8 13.5 1.0 O A:HOH1158 4.9 28.7 1.0 CE1 A:TYR117 5.0 12.3 1.0 OG A:SER494 5.0 12.8 1.0 CA A:GLY125 5.0 12.7 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei


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 E198A Variant of Catalase-Peroxidase Katg of Burkholderia Pseudomallei within 5.0Å range: probe atom residue distance (Å) B Occ B:Na802 b:20.1 occ:1.00 O B:GLY124 2.4 15.1 1.0 O B:GLY122 2.5 13.9 1.0 O B:HOH1027 2.6 25.3 1.0 O B:SER494 2.7 19.4 1.0 O B:HOH1600 2.7 29.3 1.0 C B:SER494 3.3 17.1 1.0 C B:ARG123 3.5 13.0 1.0 N B:GLY124 3.5 13.4 1.0 C B:GLY124 3.5 14.9 1.0 CA B:ARG123 3.5 12.9 1.0 C B:GLY122 3.6 12.5 1.0 O B:HOH1617 3.9 21.2 1.0 CA B:SER494 3.9 14.6 1.0 O B:HOH1014 4.0 36.9 1.0 N B:ARG123 4.0 13.1 1.0 CA B:GLY124 4.1 13.2 1.0 CB B:SER494 4.1 15.1 1.0 O B:ARG123 4.1 13.9 1.0 N B:ASP495 4.2 13.8 1.0 OD2 B:ASP427 4.2 18.2 1.0 CB B:ASP427 4.4 15.4 1.0 O B:HOH1588 4.4 35.2 1.0 CA B:ASP495 4.5 13.8 1.0 CB B:ASP495 4.6 13.1 1.0 N B:GLY125 4.7 13.4 1.0 CD1 B:TYR117 4.7 13.9 1.0 CB B:ARG123 4.8 14.8 1.0 CA B:GLY122 4.9 12.6 1.0 CG B:ASP427 4.9 16.3 1.0 CE1 B:TYR117 5.0 14.5 1.0 OG B:SER494 5.0 15.1 1.0

B.Wiseman, X.Carpena, M.Feliz, L.J.Donald, M.Pons, I.Fita, P.C.Loewen. Isonicotinic Acid Hydrazide Conversion to Isonicotinyl-Nad By Catalase-Peroxidases. J. Biol. Chem. V. 285 26662 2010.
ISSN: ESSN 1083-351X
PubMed: 20554537
DOI: 10.1074/JBC.M110.139428