Manganese in PDB 8kb3: Superoxide Dismutase

All present enzymatic activity of Superoxide Dismutase:
1.15.1.1;

The structure of Superoxide Dismutase, PDB code: 8kb3 was solved by L.Zhai, B.Q.Li, H.H.Jia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.28 / 1.62
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.026, 45.128, 92.508, 90, 90.16, 90
R / Rfree (%)	17.4 / 20.6

The binding sites of Manganese atom in the Superoxide Dismutase (pdb code 8kb3). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Superoxide Dismutase, PDB code: 8kb3:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn304 b:10.5 occ:0.62 O A:HOH457 1.9 15.1 1.0 OD2 A:ASP168 1.9 9.3 1.0 NE2 A:HIS172 2.1 9.6 1.0 NE2 A:HIS27 2.1 15.8 1.0 NE2 A:HIS82 2.2 13.7 1.0 CE1 A:HIS82 2.9 13.1 1.0 CG A:ASP168 3.0 11.3 1.0 CD2 A:HIS172 3.0 11.3 1.0 CD2 A:HIS27 3.1 15.7 1.0 CE1 A:HIS27 3.1 14.3 1.0 CE1 A:HIS172 3.1 9.9 1.0 CD2 A:HIS82 3.3 20.6 1.0 OD1 A:ASP168 3.4 7.8 1.0 ND1 A:HIS82 4.1 10.9 1.0 NE2 A:GLN147 4.1 8.2 1.0 CG A:HIS172 4.2 8.1 1.0 ND1 A:HIS27 4.2 14.1 1.0 CG A:HIS27 4.2 11.5 1.0 ND1 A:HIS172 4.2 9.2 1.0 CB A:ASP168 4.2 7.3 1.0 CZ2 A:TRP129 4.3 9.3 1.0 CG A:HIS82 4.3 10.5 1.0 CB A:TRP170 4.4 7.6 1.0 CG A:TRP170 4.5 7.1 1.0 CD1 A:TRP170 4.8 7.5 1.0 CE2 A:TYR35 4.9 8.7 1.0 CH2 A:TRP129 4.9 10.1 1.0 CB A:ALA173 4.9 8.5 1.0 OH A:TYR35 4.9 13.3 1.0

Manganese binding site 2 out of 2 in the Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn303 b:10.6 occ:0.65 OD2 B:ASP168 1.9 9.3 1.0 O B:HOH462 2.0 9.7 1.0 NE2 B:HIS82 2.1 10.4 1.0 NE2 B:HIS27 2.1 11.5 1.0 NE2 B:HIS172 2.2 11.8 1.0 CG B:ASP168 2.9 9.4 1.0 CE1 B:HIS82 2.9 12.3 1.0 CD2 B:HIS27 3.1 12.1 1.0 CD2 B:HIS172 3.1 11.6 1.0 CE1 B:HIS27 3.1 9.8 1.0 CD2 B:HIS82 3.1 11.8 1.0 CE1 B:HIS172 3.2 11.1 1.0 OD1 B:ASP168 3.4 9.8 1.0 ND1 B:HIS82 4.1 10.2 1.0 ND1 B:HIS27 4.2 9.3 1.0 CG B:HIS27 4.2 9.3 1.0 CB B:ASP168 4.2 8.0 1.0 CG B:HIS82 4.2 8.9 1.0 CG B:HIS172 4.3 9.6 1.0 NE2 B:GLN147 4.3 10.8 1.0 CZ2 B:TRP129 4.3 10.7 1.0 ND1 B:HIS172 4.3 10.4 1.0 CB B:TRP170 4.5 11.4 1.0 CG B:TRP170 4.6 10.0 1.0 CB B:ALA173 4.8 9.6 1.0 CE2 B:TYR35 4.8 11.3 1.0 CD1 B:TRP170 4.8 9.2 1.0 CH2 B:TRP129 4.9 10.6 1.0 OH B:TYR35 4.9 12.5 1.0

L.Zhai, B.Q.Li, H.H.Jia. Ydiu Regulates Salmonella Oxidative Stress By Umpylation of Soda To Be Published.