Manganese in PDB 6ex5: Staphylococcus Aureus Triple Mutant of Superoxide Dismutase Sodm

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

The structure of Staphylococcus Aureus Triple Mutant of Superoxide Dismutase Sodm, PDB code: 6ex5 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)	43.12 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.979, 58.206, 128.379, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 21.6

The binding sites of Manganese atom in the Staphylococcus Aureus Triple Mutant of Superoxide Dismutase Sodm (pdb code 6ex5). 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 Triple Mutant of Superoxide Dismutase Sodm, PDB code: 6ex5:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Staphylococcus Aureus Triple Mutant of 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 Triple Mutant of Superoxide Dismutase Sodm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:15.4 occ:1.00 OD2 A:ASP161 2.0 15.8 1.0 NE2 A:HIS81 2.2 14.2 1.0 NE2 A:HIS27 2.2 13.5 1.0 NE2 A:HIS165 2.2 13.5 1.0 O A:HOH368 2.2 16.2 1.0 CG A:ASP161 3.1 15.4 1.0 CD2 A:HIS27 3.1 13.9 1.0 CD2 A:HIS81 3.1 14.2 1.0 CD2 A:HIS165 3.2 13.5 1.0 CE1 A:HIS81 3.2 14.3 1.0 CE1 A:HIS165 3.2 13.8 1.0 CE1 A:HIS27 3.2 14.1 1.0 OD1 A:ASP161 3.5 16.9 1.0 ND1 A:HIS81 4.3 14.2 1.0 CG A:HIS27 4.3 14.4 1.0 CG A:HIS81 4.3 14.6 1.0 ND1 A:HIS165 4.3 14.2 1.0 ND1 A:HIS27 4.3 14.1 1.0 CG A:HIS165 4.3 14.1 1.0 CB A:ASP161 4.3 15.2 1.0 CZ2 A:TRP128 4.4 15.1 1.0 CB A:TRP163 4.6 15.8 1.0 CG A:TRP163 4.8 16.1 1.0 NE2 A:GLN146 4.8 16.6 1.0 CB A:ALA166 4.8 17.2 1.0 CH2 A:TRP128 5.0 15.1 1.0

Manganese binding site 2 out of 2 in the Staphylococcus Aureus Triple Mutant of 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 Triple Mutant of Superoxide Dismutase Sodm within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:16.7 occ:1.00 OD2 B:ASP161 2.0 15.9 1.0 NE2 B:HIS27 2.2 18.9 1.0 NE2 B:HIS165 2.2 17.1 1.0 NE2 B:HIS81 2.2 15.5 1.0 O B:HOH371 2.3 21.0 1.0 CG B:ASP161 3.1 16.5 1.0 CD2 B:HIS27 3.1 18.1 1.0 CD2 B:HIS81 3.1 15.7 1.0 CD2 B:HIS165 3.2 16.7 1.0 CE1 B:HIS27 3.2 17.5 1.0 CE1 B:HIS165 3.2 17.2 1.0 CE1 B:HIS81 3.2 16.2 1.0 OD1 B:ASP161 3.5 15.8 1.0 ND1 B:HIS27 4.3 18.4 1.0 CG B:HIS27 4.3 18.2 1.0 ND1 B:HIS165 4.3 17.3 1.0 CG B:HIS165 4.3 16.9 1.0 CG B:HIS81 4.3 15.8 1.0 ND1 B:HIS81 4.3 16.3 1.0 CB B:ASP161 4.3 16.5 1.0 CZ2 B:TRP128 4.4 18.5 1.0 CB B:TRP163 4.6 15.6 1.0 NE2 B:GLN146 4.7 16.4 1.0 CB B:ALA166 4.8 15.7 1.0 CG B:TRP163 4.8 15.5 1.0

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