Manganese in PDB 5n57: Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm

All present enzymatic activity of Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm:
1.15.1.1;

The structure of Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm, PDB code: 5n57 was solved by A.Barwinska-Sendra, A.Basle, K.Waldron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.55 / 2.30
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	142.225, 142.225, 46.426, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 23.7

The binding sites of Manganese atom in the Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm (pdb code 5n57). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm, PDB code: 5n57:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:29.4 occ:1.00 OD2 A:ASP161 2.0 33.3 1.0 O A:HOH323 2.2 25.1 1.0 NE2 A:HIS165 2.3 34.7 1.0 NE2 A:HIS81 2.3 30.8 1.0 NE2 A:HIS27 2.4 34.0 1.0 CG A:ASP161 3.1 34.4 1.0 CD2 A:HIS81 3.2 31.9 1.0 CE1 A:HIS165 3.2 34.4 1.0 CE1 A:HIS27 3.2 33.4 1.0 CD2 A:HIS165 3.3 34.7 1.0 CD2 A:HIS27 3.3 32.6 1.0 CE1 A:HIS81 3.4 31.9 1.0 OD1 A:ASP161 3.5 36.8 1.0 CZ2 A:TRP128 4.3 38.1 1.0 ND1 A:HIS165 4.4 35.0 1.0 ND1 A:HIS27 4.4 32.6 1.0 CG A:HIS81 4.4 31.4 1.0 CB A:ASP161 4.4 33.7 1.0 CG A:HIS165 4.4 34.8 1.0 ND1 A:HIS81 4.4 30.1 1.0 CG A:HIS27 4.4 32.5 1.0 CB A:TRP163 4.5 30.6 1.0 CH2 A:TRP128 4.6 37.0 1.0 NE2 A:GLN146 4.7 31.9 1.0 CG A:TRP163 4.7 29.0 1.0 CB A:ALA166 4.9 34.8 1.0 CD1 A:TRP163 5.0 28.5 1.0

Manganese binding site 2 out of 2 in the Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Staphylococcus Aureus Cambialistic Superoxide Dismutase Sodm within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:30.8 occ:1.00 OD2 B:ASP161 1.9 27.3 1.0 O B:HOH319 2.1 33.8 1.0 NE2 B:HIS81 2.3 38.8 1.0 NE2 B:HIS165 2.3 40.2 1.0 NE2 B:HIS27 2.4 28.2 1.0 CG B:ASP161 3.0 29.3 1.0 CD2 B:HIS81 3.2 39.3 1.0 CE1 B:HIS27 3.2 28.9 1.0 CE1 B:HIS165 3.2 41.5 1.0 CE1 B:HIS81 3.3 40.2 1.0 CD2 B:HIS165 3.3 38.8 1.0 CD2 B:HIS27 3.4 29.7 1.0 OD1 B:ASP161 3.5 28.8 1.0 CZ2 B:TRP128 4.3 33.6 1.0 CB B:ASP161 4.3 28.1 1.0 CG B:HIS81 4.3 37.8 1.0 ND1 B:HIS27 4.4 32.1 1.0 ND1 B:HIS81 4.4 39.5 1.0 ND1 B:HIS165 4.4 41.4 1.0 CG B:HIS27 4.5 30.6 1.0 CG B:HIS165 4.5 40.0 1.0 CH2 B:TRP128 4.5 29.2 1.0 CB B:TRP163 4.5 29.7 1.0 CG B:TRP163 4.7 27.8 1.0 NE2 B:GLN146 4.8 29.6 1.0 CB B:ALA166 4.9 38.9 1.0

A.Barwinska-Sendra, A.Basle, K.J.Waldron, S.Un. A Charge Polarization Model For the Metal-Specific Activity of Superoxide Dismutases. Phys Chem Chem Phys V. 20 2363 2018.
ISSN: ESSN 1463-9084
PubMed: 29308487
DOI: 10.1039/C7CP06829H