Manganese in PDB 5ag2: Sod-3 Azide Complex

All present enzymatic activity of Sod-3 Azide Complex:
1.15.1.1;

The structure of Sod-3 Azide Complex, PDB code: 5ag2 was solved by G.J.Hunter, C.H.Trinh, R.Bonetta, E.E.Stewart, D.E.Cabelli, T.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.58 / 1.77
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	82.060, 82.060, 137.610, 90.00, 90.00, 90.00
R / Rfree (%)	18.455 / 21.573

The binding sites of Manganese atom in the Sod-3 Azide Complex (pdb code 5ag2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Sod-3 Azide Complex, PDB code: 5ag2:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Sod-3 Azide Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Sod-3 Azide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn195 b:17.3 occ:1.00 OD2 A:ASP155 2.0 18.7 1.0 NE2 A:HIS74 2.2 19.2 1.0 NE2 A:HIS159 2.2 17.2 1.0 O A:HOH2096 2.2 17.6 1.0 NE2 A:HIS26 2.2 17.9 1.0 N3 A:AZI196 2.8 17.1 0.3 CG A:ASP155 3.1 17.1 1.0 CE1 A:HIS74 3.1 19.5 1.0 N2 A:AZI196 3.1 16.9 0.3 CD2 A:HIS159 3.1 17.9 1.0 CD2 A:HIS74 3.2 20.3 1.0 CE1 A:HIS26 3.2 18.0 1.0 CE1 A:HIS159 3.2 17.5 1.0 CD2 A:HIS26 3.2 18.2 1.0 OD1 A:ASP155 3.5 16.6 1.0 N1 A:AZI196 3.9 16.6 0.3 ND1 A:HIS74 4.2 19.6 1.0 CG A:HIS74 4.3 20.0 1.0 ND1 A:HIS159 4.3 17.2 1.0 CG A:HIS159 4.3 17.5 1.0 ND1 A:HIS26 4.3 19.0 1.0 CG A:HIS26 4.4 18.7 1.0 CB A:ASP155 4.4 18.2 1.0 CZ2 A:TRP122 4.5 19.9 1.0 NE2 A:GLN142 4.5 16.3 1.0 CB A:TRP157 4.6 16.1 1.0 CG A:TRP157 4.7 15.9 1.0 O A:HOH2048 5.0 17.4 0.5

Manganese binding site 2 out of 2 in the Sod-3 Azide Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Sod-3 Azide Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn195 b:19.8 occ:1.00 NE2 C:HIS159 2.1 20.0 1.0 OD2 C:ASP155 2.1 20.1 1.0 O C:HOH2108 2.2 17.1 1.0 NE2 C:HIS26 2.2 20.2 1.0 NE2 C:HIS74 2.2 21.6 1.0 N3 C:AZI196 2.6 14.4 0.3 CE1 C:HIS159 3.1 20.2 1.0 CE1 C:HIS26 3.1 21.6 1.0 CE1 C:HIS74 3.1 21.4 1.0 CD2 C:HIS159 3.1 21.2 1.0 N2 C:AZI196 3.2 14.4 0.3 CG C:ASP155 3.2 19.9 1.0 CD2 C:HIS74 3.2 22.3 1.0 CD2 C:HIS26 3.2 21.5 1.0 OD1 C:ASP155 3.6 18.7 1.0 N1 C:AZI196 4.0 14.1 0.3 ND1 C:HIS159 4.2 20.9 1.0 ND1 C:HIS26 4.2 22.3 1.0 ND1 C:HIS74 4.3 21.1 1.0 CG C:HIS159 4.3 21.0 1.0 CG C:HIS26 4.3 22.3 1.0 CG C:HIS74 4.3 21.9 1.0 CB C:ASP155 4.4 20.3 1.0 NE2 C:GLN142 4.5 16.8 1.0 CZ2 C:TRP122 4.5 19.5 1.0 CB C:TRP157 4.6 18.9 1.0 CG C:TRP157 4.7 18.8 1.0 O C:HOH2049 4.9 32.1 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: ISSN 0961-8368
PubMed: 26257399
DOI: 10.1002/PRO.2768