Sodium in PDB 5sx0: Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5

All present enzymatic activity of Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5:
1.11.1.21;

The structure of Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5, PDB code: 5sx0 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 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	100.359, 114.886, 174.626, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 19.4

The structure of Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 (pdb code 5sx0). 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 An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5, PDB code: 5sx0:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5


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 An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na802 b:24.1 occ:1.00 O A:SER494 2.3 22.1 1.0 O A:GLY124 2.3 21.7 1.0 O A:GLY122 2.4 23.0 1.0 O A:HOH915 2.4 22.9 1.0 O A:HOH1257 2.5 32.9 1.0 C A:SER494 3.2 20.5 1.0 C A:GLY124 3.5 20.0 1.0 C A:GLY122 3.5 20.5 1.0 C A:ARG123 3.6 19.6 1.0 CA A:ARG123 3.6 20.1 1.0 N A:GLY124 3.6 20.3 1.0 OD2 A:ASP427 4.0 19.2 1.0 CA A:SER494 4.0 19.6 1.0 N A:ASP495 4.0 20.8 1.0 O A:HOH1146 4.0 33.2 1.0 N A:ARG123 4.1 20.2 1.0 CB A:ASP427 4.1 20.8 1.0 O A:HOH1148 4.1 22.4 1.0 CA A:GLY124 4.2 20.2 1.0 O A:ARG123 4.2 18.8 1.0 CB A:SER494 4.2 20.0 1.0 CA A:ASP495 4.3 20.0 1.0 CB A:ASP495 4.5 19.2 1.0 CG A:ASP427 4.5 20.4 1.0 N A:GLY125 4.6 20.8 1.0 CD1 A:TYR117 4.7 20.0 1.0 OE2 A:GLU198 4.7 56.1 1.0 CA A:GLY122 4.8 20.7 1.0 CA A:GLY125 4.9 19.5 1.0 CB A:ARG123 4.9 22.6 1.0 OE1 A:GLU198 4.9 37.5 1.0 CE1 A:TYR117 4.9 20.7 1.0 OG A:SER494 5.0 19.4 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5


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 An Oxoferryl Species of Catalase-Peroxidase Katg at PH7.5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Na802 b:25.8 occ:1.00 O B:HOH2025 2.3 23.2 1.0 O B:SER494 2.3 22.8 1.0 O B:GLY122 2.3 20.5 1.0 O B:GLY124 2.3 21.0 1.0 O B:HOH2233 2.4 27.5 1.0 C B:SER494 3.1 20.2 1.0 C B:GLY124 3.5 19.4 1.0 C B:GLY122 3.5 19.2 1.0 C B:ARG123 3.6 19.7 1.0 N B:GLY124 3.6 19.7 1.0 CA B:ARG123 3.6 19.6 1.0 CA B:SER494 4.0 18.8 1.0 N B:ASP495 4.0 18.5 1.0 OD2 B:ASP427 4.0 20.2 1.0 CB B:ASP427 4.0 21.1 1.0 O B:HOH2322 4.0 34.4 1.0 O B:HOH2285 4.1 21.7 1.0 N B:ARG123 4.1 19.9 1.0 CB B:SER494 4.2 19.2 1.0 CA B:GLY124 4.2 20.7 1.0 O B:ARG123 4.2 19.0 1.0 CA B:ASP495 4.3 17.9 1.0 CB B:ASP495 4.5 19.1 1.0 CG B:ASP427 4.5 21.4 1.0 N B:GLY125 4.7 19.5 1.0 CD1 B:TYR117 4.7 20.6 1.0 OE2 B:GLU198 4.7 44.0 1.0 CA B:GLY122 4.8 19.4 1.0 CB B:ARG123 4.9 20.8 1.0 CE1 B:TYR117 4.9 19.8 1.0 OG B:SER494 4.9 18.3 1.0 CA B:GLY125 5.0 19.8 1.0

X.Carpena, B.Wiseman, T.Deemagarn, R.Singh, J.Switala, A.Ivancich, I.Fita, P.C.Loewen. A Molecular Switch and Electronic Circuit Modulate Catalase Activity in Catalase-Peroxidases. Embo Rep. V. 6 1156 2005.
ISSN: ISSN 1469-221X
PubMed: 16211084