Manganese in PDB 1zlz: Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase

All present enzymatic activity of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase:
1.15.1.1;

The structure of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase, PDB code: 1zlz was solved by J.R.Salvador, M.M.Whittaker, J.W.Whittaker, G.B.Jameson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.69 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.727, 45.676, 95.859, 90.00, 97.92, 90.00
R / Rfree (%)	18.2 / 22.2

The binding sites of Manganese atom in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase (pdb code 1zlz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase, PDB code: 1zlz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn206 b:16.1 occ:1.00 MN A:MH2206 0.0 16.1 1.0 OD2 A:ASP167 2.0 17.9 1.0 NE2 A:HIS81 2.1 18.1 1.0 NE2 A:HIS171 2.2 16.3 1.0 NE2 A:HIS26 2.2 12.3 1.0 O1 A:MH2206 2.3 15.0 1.0 CG A:ASP167 3.1 13.9 1.0 CE1 A:HIS26 3.1 9.4 1.0 CD2 A:HIS81 3.1 20.5 1.0 CE1 A:HIS81 3.1 16.1 1.0 CE1 A:HIS171 3.1 15.1 1.0 CD2 A:HIS171 3.1 14.6 1.0 CD2 A:HIS26 3.2 18.9 1.0 OD1 A:ASP167 3.4 15.5 1.0 ND1 A:HIS81 4.2 14.8 1.0 CG A:HIS81 4.2 16.3 1.0 ND1 A:HIS26 4.3 15.1 1.0 ND1 A:HIS171 4.3 15.9 1.0 CG A:HIS171 4.3 16.2 1.0 CG A:HIS26 4.3 12.4 1.0 CB A:ASP167 4.3 13.3 1.0 CZ2 A:TRP128 4.6 15.2 1.0 CB A:TRP169 4.6 17.7 1.0 NE2 A:GLN146 4.7 14.4 1.0 CG A:TRP169 4.9 17.3 1.0 CB A:ALA172 4.9 15.3 1.0

Manganese binding site 2 out of 2 in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn206 b:17.1 occ:1.00 MN B:MH2206 0.0 17.1 1.0 N3 B:AZI1207 1.9 28.0 1.0 OD2 B:ASP167 2.0 16.8 1.0 NE2 B:HIS81 2.1 16.6 1.0 O1 B:MH2206 2.1 15.8 1.0 NE2 B:HIS171 2.2 20.5 1.0 NE2 B:HIS26 2.2 16.4 1.0 N2 B:AZI1207 2.9 29.0 1.0 CE1 B:HIS26 3.0 18.4 1.0 CD2 B:HIS81 3.1 18.4 1.0 CE1 B:HIS171 3.1 20.8 1.0 CG B:ASP167 3.1 13.0 1.0 CE1 B:HIS81 3.1 19.9 1.0 CD2 B:HIS171 3.2 16.1 1.0 CD2 B:HIS26 3.3 15.4 1.0 OD1 B:ASP167 3.5 18.7 1.0 N1 B:AZI1207 4.0 22.8 1.0 ND1 B:HIS26 4.2 16.7 1.0 ND1 B:HIS81 4.2 18.3 1.0 CG B:HIS81 4.2 15.9 1.0 ND1 B:HIS171 4.2 15.3 1.0 CG B:HIS171 4.3 16.6 1.0 CG B:HIS26 4.3 14.3 1.0 CB B:ASP167 4.4 17.6 1.0 NE2 B:GLN146 4.7 17.4 1.0 CB B:TRP169 4.7 17.6 1.0 CZ2 B:TRP128 4.7 15.2 1.0 CG B:TRP169 4.8 13.9 1.0 O B:HOH208 4.9 24.5 1.0

J.R.Salvador, M.M.Whittaker, J.W.Whittaker, G.B.Jameson. Azide Adduct of the Y174F Mutant of Manganese Superoxide Dismutase From Escherichia Coli To Be Published.