Iron in PDB 6ex3: Staphylococcus Aureus Superoxide Dismutase Soda

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

The structure of Staphylococcus Aureus Superoxide Dismutase Soda, PDB code: 6ex3 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)	47.01 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.557, 66.381, 108.311, 90.00, 98.72, 90.00
R / Rfree (%)	20.1 / 26.7

The binding sites of Iron atom in the Staphylococcus Aureus Superoxide Dismutase Soda (pdb code 6ex3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Staphylococcus Aureus Superoxide Dismutase Soda, PDB code: 6ex3:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Staphylococcus Aureus Superoxide Dismutase Soda


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Staphylococcus Aureus Superoxide Dismutase Soda within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:38.1 occ:1.00 NE2 A:HIS81 2.0 29.4 1.0 OD2 A:ASP161 2.1 33.2 1.0 O A:HOH307 2.1 24.4 1.0 NE2 A:HIS27 2.3 32.5 1.0 NE2 A:HIS165 2.3 25.3 1.0 CE1 A:HIS81 2.9 32.2 1.0 CD2 A:HIS81 3.0 30.4 1.0 CG A:ASP161 3.1 29.2 1.0 CD2 A:HIS27 3.2 31.9 1.0 CD2 A:HIS165 3.3 27.2 1.0 CE1 A:HIS27 3.3 33.9 1.0 CE1 A:HIS165 3.3 25.3 1.0 OD1 A:ASP161 3.4 25.2 1.0 ND1 A:HIS81 4.0 31.4 1.0 CG A:HIS81 4.1 32.8 1.0 CB A:ASP161 4.3 31.1 1.0 CZ2 A:TRP128 4.4 29.6 1.0 ND1 A:HIS27 4.4 30.5 1.0 CG A:HIS27 4.4 31.4 1.0 CG A:HIS165 4.4 27.1 1.0 ND1 A:HIS165 4.4 26.2 1.0 CB A:TRP163 4.5 22.3 1.0 NE2 A:GLN146 4.6 31.3 1.0 CG A:TRP163 4.6 21.8 1.0 CD1 A:TRP163 4.9 22.1 1.0 CH2 A:TRP128 4.9 30.1 1.0 OH A:TYR35 4.9 46.9 1.0 CB A:ALA166 5.0 27.8 1.0

Iron binding site 2 out of 4 in the Staphylococcus Aureus Superoxide Dismutase Soda


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Staphylococcus Aureus Superoxide Dismutase Soda within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:38.6 occ:1.00 NE2 B:HIS81 2.0 24.4 1.0 OD2 B:ASP161 2.1 28.9 1.0 O B:HOH322 2.1 19.8 1.0 NE2 B:HIS27 2.1 28.9 1.0 NE2 B:HIS165 2.4 25.4 1.0 CE1 B:HIS81 3.0 23.7 1.0 CD2 B:HIS81 3.0 25.8 1.0 CG B:ASP161 3.1 29.2 1.0 CE1 B:HIS27 3.1 28.5 1.0 CD2 B:HIS27 3.1 28.0 1.0 CD2 B:HIS165 3.3 24.4 1.0 CE1 B:HIS165 3.3 23.3 1.0 OD1 B:ASP161 3.4 24.8 1.0 ND1 B:HIS81 4.1 23.9 1.0 CG B:HIS81 4.1 25.5 1.0 ND1 B:HIS27 4.2 26.5 1.0 CG B:HIS27 4.2 28.1 1.0 CB B:ASP161 4.3 30.3 1.0 CZ2 B:TRP128 4.4 25.2 1.0 ND1 B:HIS165 4.4 24.9 1.0 CG B:HIS165 4.4 25.2 1.0 OE1 B:GLN146 4.7 27.4 1.0 CB B:TRP163 4.7 25.5 1.0 CG B:TRP163 4.8 26.0 1.0 OH B:TYR35 4.9 47.3 1.0 CH2 B:TRP128 4.9 25.4 1.0 CB B:ALA166 5.0 29.0 1.0

Iron binding site 3 out of 4 in the Staphylococcus Aureus Superoxide Dismutase Soda


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Staphylococcus Aureus Superoxide Dismutase Soda within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:33.5 occ:1.00 OD2 C:ASP161 1.9 27.6 1.0 NE2 C:HIS165 2.2 28.9 1.0 NE2 C:HIS81 2.2 18.6 1.0 O C:HOH315 2.2 16.6 1.0 NE2 C:HIS27 2.2 25.9 1.0 CG C:ASP161 3.0 22.9 1.0 CE1 C:HIS81 3.1 21.1 1.0 CD2 C:HIS165 3.1 31.4 1.0 CE1 C:HIS27 3.1 26.6 1.0 CE1 C:HIS165 3.2 29.1 1.0 CD2 C:HIS27 3.2 25.1 1.0 CD2 C:HIS81 3.2 21.2 1.0 OD1 C:ASP161 3.3 21.3 1.0 ND1 C:HIS81 4.2 20.9 1.0 ND1 C:HIS27 4.3 25.6 1.0 CB C:ASP161 4.3 26.2 1.0 CG C:HIS165 4.3 31.8 1.0 ND1 C:HIS165 4.3 29.9 1.0 CG C:HIS81 4.3 23.9 1.0 CG C:HIS27 4.3 24.3 1.0 CZ2 C:TRP128 4.4 25.2 1.0 NE2 C:GLN146 4.5 28.7 1.0 CB C:TRP163 4.5 25.1 1.0 OH C:TYR35 4.7 41.3 1.0 CG C:TRP163 4.7 23.7 1.0 CB C:ALA166 4.8 31.5 1.0 CD1 C:TRP163 5.0 24.1 1.0

Iron binding site 4 out of 4 in the Staphylococcus Aureus Superoxide Dismutase Soda


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Staphylococcus Aureus Superoxide Dismutase Soda within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:33.8 occ:1.00 O D:HOH316 2.0 16.3 1.0 OD2 D:ASP161 2.0 28.6 1.0 NE2 D:HIS81 2.1 22.1 1.0 NE2 D:HIS27 2.1 25.8 1.0 NE2 D:HIS165 2.2 27.4 1.0 CE1 D:HIS81 3.0 23.3 1.0 CG D:ASP161 3.0 23.0 1.0 CE1 D:HIS27 3.1 24.3 1.0 CD2 D:HIS81 3.1 24.5 1.0 CE1 D:HIS165 3.1 24.9 1.0 CD2 D:HIS27 3.1 24.2 1.0 CD2 D:HIS165 3.2 27.6 1.0 OD1 D:ASP161 3.4 23.1 1.0 ND1 D:HIS81 4.1 23.9 1.0 ND1 D:HIS27 4.2 21.8 1.0 CG D:HIS81 4.2 26.1 1.0 CB D:ASP161 4.3 24.5 1.0 ND1 D:HIS165 4.3 27.1 1.0 CG D:HIS27 4.3 24.0 1.0 CG D:HIS165 4.3 24.8 1.0 CZ2 D:TRP128 4.4 26.5 1.0 NE2 D:GLN146 4.6 30.7 1.0 OH D:TYR35 4.6 52.0 1.0 CB D:TRP163 4.7 25.2 1.0 CG D:TRP163 4.9 26.9 1.0 CH2 D:TRP128 5.0 27.7 1.0 CB D:ALA166 5.0 25.5 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.