Manganese in PDB 6qv9: Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant

All present enzymatic activity of Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant:
1.15.1.1;

The structure of Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant, PDB code: 6qv9 was solved by A.Basle, A.Barwinska-Sendra, K.Waldron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.77 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.250, 68.150, 57.290, 90.00, 100.58, 90.00
R / Rfree (%)	17.1 / 20.7

The binding sites of Manganese atom in the Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant (pdb code 6qv9). 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 Superoxide Dismutase Soda Double Mutant, PDB code: 6qv9:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:11.7 occ:1.00 OD2 A:ASP161 2.0 15.3 1.0 NE2 A:HIS165 2.1 11.2 1.0 NE2 A:HIS81 2.1 12.4 1.0 NE2 A:HIS27 2.2 11.5 1.0 O A:HOH343 2.3 14.7 1.0 CG A:ASP161 3.0 13.5 1.0 CE1 A:HIS81 3.1 14.5 1.0 CE1 A:HIS165 3.1 11.8 1.0 CD2 A:HIS81 3.1 12.0 1.0 CE1 A:HIS27 3.1 11.6 1.0 CD2 A:HIS165 3.1 11.5 1.0 CD2 A:HIS27 3.2 11.8 1.0 OD1 A:ASP161 3.5 13.6 1.0 ND1 A:HIS81 4.2 13.0 1.0 ND1 A:HIS165 4.2 13.4 1.0 ND1 A:HIS27 4.2 11.7 1.0 CG A:HIS81 4.2 12.8 1.0 CG A:HIS165 4.2 11.0 1.0 CG A:HIS27 4.3 12.5 1.0 CZ2 A:TRP128 4.3 12.1 1.0 CB A:ASP161 4.3 13.3 1.0 CB A:TRP163 4.5 11.4 1.0 CH2 A:TRP128 4.7 13.0 1.0 CG A:TRP163 4.7 10.6 1.0 NE2 A:GLN146 4.9 14.6 1.0 CB A:ALA166 5.0 11.3 1.0

Manganese binding site 2 out of 2 in the Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Staphylococcus Aureus Superoxide Dismutase Soda Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:10.6 occ:1.00 OD2 B:ASP161 1.9 12.6 1.0 NE2 B:HIS81 2.1 11.2 1.0 NE2 B:HIS27 2.1 9.8 1.0 NE2 B:HIS165 2.2 12.5 1.0 O B:HOH337 2.3 13.8 1.0 CG B:ASP161 3.0 11.2 1.0 CE1 B:HIS27 3.0 10.6 1.0 CD2 B:HIS81 3.1 11.2 1.0 CE1 B:HIS81 3.1 12.0 1.0 CD2 B:HIS27 3.2 11.3 1.0 CD2 B:HIS165 3.2 12.3 1.0 CE1 B:HIS165 3.2 13.1 1.0 OD1 B:ASP161 3.5 12.2 1.0 ND1 B:HIS27 4.2 11.3 1.0 ND1 B:HIS81 4.2 10.9 1.0 CG B:HIS81 4.2 11.1 1.0 CG B:HIS27 4.3 10.6 1.0 CZ2 B:TRP128 4.3 12.8 1.0 ND1 B:HIS165 4.3 13.2 1.0 CB B:ASP161 4.3 12.6 1.0 CG B:HIS165 4.3 12.2 1.0 CH2 B:TRP128 4.6 13.2 1.0 CB B:TRP163 4.7 10.8 1.0 CG B:TRP163 4.9 10.6 1.0 CB B:ALA166 4.9 10.9 1.0 NE2 B:GLN146 4.9 15.0 1.0

A.Barwinska-Sendra, Y.M.Garcia, A.Basle, E.Tarrant, K.Sendra, C.Bicep, S.Un, T.E.Khel-Fie, K.J.Waldron. An Evolutionary Path to Altered Cofactor Specificity in A Metalloenzyme To Be Published.