Manganese in PDB 1n0n: Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase

All present enzymatic activity of Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase:
1.15.1.1;

The structure of Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase, PDB code: 1n0n was solved by G.E.O.Borgstahl, H.E.Parge, M.J.Hickey, W.F.Beyer Jr., R.A.Hallewell, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 1.82
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	79.815, 79.815, 240.882, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 24.1

The binding sites of Manganese atom in the Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase (pdb code 1n0n). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase, PDB code: 1n0n:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn199 b:15.4 occ:1.00 OD1 A:ASP159 2.1 15.0 1.0 O A:HOH769 2.1 15.2 1.0 NE2 A:HIS163 2.1 14.3 1.0 NE2 A:HIS26 2.2 15.6 1.0 NE2 A:HIS74 2.2 15.2 1.0 CE1 A:HIS163 3.0 14.7 1.0 CG A:ASP159 3.1 15.3 1.0 CE1 A:HIS26 3.1 15.8 1.0 CD2 A:HIS163 3.2 14.6 1.0 CE1 A:HIS74 3.2 15.5 1.0 CD2 A:HIS74 3.2 15.2 1.0 CD2 A:HIS26 3.2 16.1 1.0 OD2 A:ASP159 3.4 15.0 1.0 ND1 A:HIS163 4.2 14.5 1.0 CZ2 A:TRP123 4.2 14.9 1.0 CG A:HIS163 4.3 14.7 1.0 ND1 A:HIS26 4.3 15.9 1.0 ND1 A:HIS74 4.3 15.2 1.0 CG A:HIS74 4.4 15.4 1.0 CG A:HIS26 4.4 16.2 1.0 CB A:ASP159 4.4 15.2 1.0 NE2 A:GLN143 4.5 14.2 1.0 CB A:TRP161 4.5 14.2 1.0 CG1 A:VAL30 4.5 17.1 1.0 CG A:TRP161 4.6 14.1 1.0 CH2 A:TRP123 4.8 14.9 1.0 CB A:ALA164 4.9 15.5 1.0 CD1 A:TRP161 4.9 14.0 1.0 CE2 A:TRP123 5.0 14.9 1.0

Manganese binding site 2 out of 2 in the Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn199 b:14.3 occ:1.00 OD1 B:ASP159 2.0 14.2 1.0 NE2 B:HIS163 2.1 13.3 1.0 NE2 B:HIS74 2.2 14.1 1.0 NE2 B:HIS26 2.2 14.4 1.0 O B:HOH872 2.2 13.5 1.0 CE1 B:HIS163 3.1 13.8 1.0 CE1 B:HIS26 3.1 15.2 1.0 CG B:ASP159 3.1 15.1 1.0 CE1 B:HIS74 3.1 14.6 1.0 CD2 B:HIS74 3.1 14.6 1.0 CD2 B:HIS163 3.2 13.7 1.0 CD2 B:HIS26 3.2 15.3 1.0 OD2 B:ASP159 3.5 14.8 1.0 ND1 B:HIS163 4.2 13.6 1.0 ND1 B:HIS26 4.2 15.2 1.0 ND1 B:HIS74 4.2 14.6 1.0 CG B:HIS74 4.3 14.7 1.0 CZ2 B:TRP123 4.3 15.1 1.0 CG B:HIS163 4.3 13.7 1.0 CG B:HIS26 4.3 15.3 1.0 CG1 B:VAL30 4.4 16.1 1.0 CB B:ASP159 4.4 15.1 1.0 NE2 B:GLN143 4.5 13.7 1.0 CB B:TRP161 4.6 13.4 1.0 CG B:TRP161 4.7 13.2 1.0 CH2 B:TRP123 4.8 14.9 1.0 CB B:ALA164 4.9 15.0 1.0 CD1 B:TRP161 5.0 13.3 1.0

G.E.O.Borgstahl, H.E.Parge, M.J.Hickey, W.F.Beyer Jr., R.A.Hallewell, J.A.Tainer. Catalytic and Structural Effects of Amino-Acid Substitution at HIS30 in Human Manganese Superoxide Dismutase To Be Published.