Manganese in PDB 1n0j: The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles

All present enzymatic activity of The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles:
1.15.1.1;

The structure of The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles, PDB code: 1n0j was solved by G.E.O.Borgstahl, H.E.Parge, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.130, 79.900, 68.050, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / n/a

The binding sites of Manganese atom in the The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles (pdb code 1n0j). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles, PDB code: 1n0j:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn199 b:15.3 occ:1.00 OD1 A:ASP159 1.9 12.4 1.0 O A:HOH400 2.0 17.4 1.0 NE2 A:HIS74 2.1 15.0 1.0 NE2 A:HIS163 2.1 12.2 1.0 NE2 A:HIS26 2.1 16.2 1.0 CE1 A:HIS26 3.0 15.4 1.0 CE1 A:HIS74 3.0 13.5 1.0 CE1 A:HIS163 3.0 15.6 1.0 CG A:ASP159 3.0 13.7 1.0 CD2 A:HIS163 3.1 14.8 1.0 CD2 A:HIS74 3.1 15.8 1.0 CD2 A:HIS26 3.2 12.3 1.0 OD2 A:ASP159 3.5 10.5 1.0 ND1 A:HIS74 4.1 11.2 1.0 ND1 A:HIS26 4.1 13.5 1.0 ND1 A:HIS163 4.2 17.8 1.0 CG A:HIS74 4.2 15.0 1.0 CG A:HIS163 4.3 14.0 1.0 CG A:HIS26 4.3 14.1 1.0 CB A:ASP159 4.3 8.4 1.0 CZ2 A:TRP123 4.4 13.8 1.0 NE2 A:GLN143 4.6 12.2 1.0 CB A:TRP161 4.6 8.7 1.0 CG A:TRP161 4.7 9.1 1.0 CH2 A:TRP123 4.9 8.6 1.0 CD1 A:TRP161 5.0 7.7 1.0

Manganese binding site 2 out of 2 in the The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn199 b:16.0 occ:1.00 OD1 B:ASP159 1.9 13.1 1.0 O B:HOH401 2.0 23.1 1.0 NE2 B:HIS26 2.1 24.8 1.0 NE2 B:HIS163 2.1 12.6 1.0 NE2 B:HIS74 2.1 19.6 1.0 CE1 B:HIS74 2.9 23.4 1.0 CE1 B:HIS26 2.9 24.4 1.0 CG B:ASP159 3.0 16.0 1.0 CD2 B:HIS163 3.0 10.3 1.0 CE1 B:HIS163 3.1 10.4 1.0 CD2 B:HIS26 3.1 19.2 1.0 CD2 B:HIS74 3.2 20.1 1.0 OD2 B:ASP159 3.3 19.0 1.0 ND1 B:HIS74 4.1 21.2 1.0 ND1 B:HIS26 4.1 27.2 1.0 CG B:HIS163 4.2 11.1 1.0 ND1 B:HIS163 4.2 11.3 1.0 CG B:HIS26 4.2 26.1 1.0 CB B:ASP159 4.3 9.1 1.0 CG B:HIS74 4.3 15.1 1.0 CZ2 B:TRP123 4.5 6.9 1.0 CB B:TRP161 4.6 10.9 1.0 NE2 B:GLN143 4.7 12.3 1.0 CG B:TRP161 4.8 11.4 1.0

G.E.Borgstahl, H.E.Parge, M.J.Hickey, W.F.Beyer Jr., R.A.Hallewell, J.A.Tainer. The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals A Novel Tetrameric Interface of Two 4-Helix Bundles Cell(Cambridge,Mass.) V. 71 107 1992.
ISSN: ISSN 0092-8674
PubMed: 1394426
DOI: 10.1016/0092-8674(92)90270-M