Manganese in PDB 1ap6: TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase

All present enzymatic activity of TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase:
1.15.1.1;

The structure of TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase, PDB code: 1ap6 was solved by Y.Guan, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	80.900, 80.900, 242.500, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 23.6

The binding sites of Manganese atom in the TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase (pdb code 1ap6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase, PDB code: 1ap6:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the TYR34->Phe Mutant of Human Mitochondrial 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 TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn199 b:21.3 occ:1.00 OD2 A:ASP159 2.0 17.5 1.0 O A:HOH801 2.0 15.8 1.0 NE2 A:HIS26 2.1 17.7 1.0 NE2 A:HIS74 2.1 16.1 1.0 NE2 A:HIS163 2.2 18.3 1.0 CE1 A:HIS74 3.0 17.1 1.0 CE1 A:HIS26 3.1 17.4 1.0 CD2 A:HIS26 3.1 17.2 1.0 CE1 A:HIS163 3.1 14.9 1.0 CG A:ASP159 3.1 14.1 1.0 CD2 A:HIS74 3.2 16.0 1.0 CD2 A:HIS163 3.2 21.1 1.0 OD1 A:ASP159 3.6 12.8 1.0 ND1 A:HIS26 4.2 18.3 1.0 ND1 A:HIS74 4.2 17.4 1.0 CG A:HIS26 4.2 20.0 1.0 ND1 A:HIS163 4.2 16.2 1.0 CG A:HIS74 4.3 17.9 1.0 CB A:ASP159 4.3 14.1 1.0 CG A:HIS163 4.3 20.0 1.0 CZ2 A:TRP123 4.4 16.1 1.0 CB A:TRP161 4.6 12.9 1.0 NE2 A:GLN143 4.6 14.1 1.0 CG A:TRP161 4.7 12.7 1.0 CB A:ALA164 4.9 16.4 1.0 CH2 A:TRP123 4.9 13.9 1.0

Manganese binding site 2 out of 2 in the TYR34->Phe Mutant of Human Mitochondrial 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 TYR34->Phe Mutant of Human Mitochondrial Manganese Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn199 b:20.4 occ:1.00 OD2 B:ASP159 2.0 16.2 1.0 NE2 B:HIS74 2.0 12.6 1.0 O B:HOH802 2.1 18.0 1.0 NE2 B:HIS26 2.1 21.0 1.0 NE2 B:HIS163 2.2 19.6 1.0 CE1 B:HIS74 2.9 14.3 1.0 CE1 B:HIS26 3.0 16.0 1.0 CG B:ASP159 3.0 14.0 1.0 CE1 B:HIS163 3.1 18.0 1.0 CD2 B:HIS74 3.1 14.2 1.0 CD2 B:HIS26 3.2 14.0 1.0 CD2 B:HIS163 3.3 17.1 1.0 OD1 B:ASP159 3.5 16.5 1.0 ND1 B:HIS74 4.1 15.4 1.0 ND1 B:HIS26 4.1 15.7 1.0 CG B:HIS74 4.2 14.0 1.0 CG B:HIS26 4.3 16.3 1.0 ND1 B:HIS163 4.3 18.6 1.0 CZ2 B:TRP123 4.3 15.3 1.0 CB B:ASP159 4.3 14.0 1.0 CG B:HIS163 4.4 20.0 1.0 NE2 B:GLN143 4.6 13.4 1.0 CB B:TRP161 4.6 12.4 1.0 CH2 B:TRP123 4.7 12.2 1.0 CG B:TRP161 4.8 13.1 1.0 CB B:ALA164 5.0 11.2 1.0

Y.Guan, M.J.Hickey, G.E.Borgstahl, R.A.Hallewell, J.R.Lepock, D.O'connor, Y.Hsieh, H.S.Nick, D.N.Silverman, J.A.Tainer. Crystal Structure of Y34F Mutant Human Mitochondrial Manganese Superoxide Dismutase and the Functional Role of Tyrosine 34. Biochemistry V. 37 4722 1998.
ISSN: ISSN 0006-2960
PubMed: 9537987
DOI: 10.1021/BI972394L