Manganese in PDB 4x9q: Mnsod-3 Room Temperature Structure

All present enzymatic activity of Mnsod-3 Room Temperature Structure:
1.15.1.1;

The structure of Mnsod-3 Room Temperature Structure, PDB code: 4x9q was solved by G.J.Hunter, C.H.Trinh, T.Hunter, R.Bonetta, E.E.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.19 / 1.77
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.465, 81.465, 137.959, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 21.4

The binding sites of Manganese atom in the Mnsod-3 Room Temperature Structure (pdb code 4x9q). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Mnsod-3 Room Temperature Structure, PDB code: 4x9q:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Mnsod-3 Room Temperature Structure


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mnsod-3 Room Temperature Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:14.6 occ:1.00 OD2 A:ASP155 2.1 14.5 1.0 O A:HOH353 2.2 13.8 1.0 NE2 A:HIS74 2.2 15.6 1.0 NE2 A:HIS26 2.2 13.6 1.0 NE2 A:HIS159 2.2 13.4 1.0 CG A:ASP155 3.1 14.3 1.0 CD2 A:HIS159 3.1 14.7 1.0 CE1 A:HIS26 3.2 14.5 1.0 CE1 A:HIS74 3.2 14.9 1.0 CD2 A:HIS74 3.2 16.3 1.0 CD2 A:HIS26 3.2 13.9 1.0 CE1 A:HIS159 3.3 13.9 1.0 OD1 A:ASP155 3.5 13.9 1.0 ND1 A:HIS74 4.3 15.9 1.0 ND1 A:HIS26 4.3 15.1 1.0 CG A:HIS159 4.3 13.7 1.0 CG A:HIS74 4.3 15.3 1.0 CG A:HIS26 4.3 14.0 1.0 ND1 A:HIS159 4.3 14.2 1.0 CZ2 A:TRP122 4.3 16.1 1.0 CB A:ASP155 4.4 15.1 1.0 CB A:TRP157 4.5 13.9 1.0 NE2 A:GLN142 4.6 13.6 1.0 CG A:TRP157 4.7 13.8 1.0 CB A:ALA160 4.9 15.8 1.0 CH2 A:TRP122 4.9 16.8 1.0

Manganese binding site 2 out of 2 in the Mnsod-3 Room Temperature Structure


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Mnsod-3 Room Temperature Structure within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn201 b:16.9 occ:1.00 OD2 C:ASP155 2.0 18.1 1.0 NE2 C:HIS159 2.2 16.4 1.0 NE2 C:HIS74 2.2 17.9 1.0 NE2 C:HIS26 2.2 17.2 1.0 O C:HOH353 2.3 16.0 1.0 CD2 C:HIS159 3.1 17.1 1.0 CG C:ASP155 3.1 16.6 1.0 CE1 C:HIS26 3.2 18.6 1.0 CD2 C:HIS74 3.2 17.6 1.0 CE1 C:HIS74 3.2 16.2 1.0 CD2 C:HIS26 3.2 17.6 1.0 CE1 C:HIS159 3.2 16.4 1.0 OD1 C:ASP155 3.6 16.8 1.0 ND1 C:HIS26 4.3 18.7 1.0 ND1 C:HIS74 4.3 16.2 1.0 CG C:HIS159 4.3 17.1 1.0 CG C:HIS74 4.3 17.1 1.0 ND1 C:HIS159 4.3 17.5 1.0 CG C:HIS26 4.3 18.2 1.0 CB C:ASP155 4.4 17.0 1.0 CZ2 C:TRP122 4.4 15.9 1.0 CB C:TRP157 4.5 16.2 1.0 NE2 C:GLN142 4.6 16.4 1.0 CG C:TRP157 4.7 15.3 1.0 CB C:ALA160 4.9 18.5 1.0 CD1 C:TRP157 5.0 14.6 1.0 CH2 C:TRP122 5.0 17.3 1.0

G.J.Hunter, C.H.Trinh, R.Bonetta, E.E.Stewart, D.E.Cabelli, T.Hunter. The Structure of the Caenorhabditis Elegans Manganese Superoxide Dismutase Mnsod-3-Azide Complex. Protein Sci. V. 24 1777 2015.
ISSN: ESSN 1469-896X
PubMed: 26257399
DOI: 10.1002/PRO.2768