Manganese in PDB 1i0h: Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution.

All present enzymatic activity of Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution.:
1.15.1.1;

The structure of Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution., PDB code: 1i0h was solved by R.A.Edwards, M.M.Whittaker, J.W.Whittaker, E.N.Baker, G.B.Jameson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.893, 46.017, 95.993, 90.00, 98.40, 90.00
R / Rfree (%)	16.9 / 19.6

The binding sites of Manganese atom in the Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution. (pdb code 1i0h). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution., PDB code: 1i0h:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn206 b:5.3 occ:1.00 OD2 A:ASP167 2.0 5.7 1.0 NE2 A:HIS171 2.1 6.6 1.0 NE2 A:HIS81 2.2 5.1 1.0 NE2 A:HIS26 2.2 4.6 1.0 O A:HOH469 2.2 5.5 1.0 CG A:ASP167 3.0 3.8 1.0 CE1 A:HIS171 3.1 6.7 1.0 CD2 A:HIS171 3.1 4.5 1.0 CE1 A:HIS26 3.1 7.5 1.0 CD2 A:HIS81 3.1 4.4 1.0 CD2 A:HIS26 3.1 5.5 1.0 CE1 A:HIS81 3.2 5.2 1.0 OD1 A:ASP167 3.4 5.4 1.0 ND1 A:HIS171 4.2 6.0 1.0 ND1 A:HIS26 4.2 5.2 1.0 CG A:HIS171 4.3 6.0 1.0 ND1 A:HIS81 4.3 5.3 1.0 CG A:HIS81 4.3 4.8 1.0 CG A:HIS26 4.3 4.3 1.0 CB A:ASP167 4.3 4.3 1.0 CZ2 A:TRP128 4.4 6.2 1.0 CB A:TRP169 4.6 5.4 1.0 NE2 A:GLN146 4.7 4.8 1.0 CG A:TRP169 4.8 4.5 1.0 CB A:ALA172 4.9 5.4 1.0 CH2 A:TRP128 4.9 5.6 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the E. Coli Manganese Superoxide Dismutase Mutant Y174F at 1.35 Angstroms Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn206 b:6.9 occ:1.00 OD2 B:ASP167 2.0 6.7 1.0 NE2 B:HIS26 2.1 6.0 1.0 NE2 B:HIS171 2.2 6.3 1.0 NE2 B:HIS81 2.2 7.2 1.0 O B:HOH443 2.2 8.2 1.0 CG B:ASP167 3.0 5.8 1.0 CE1 B:HIS26 3.1 6.4 1.0 CE1 B:HIS171 3.1 6.5 1.0 CE1 B:HIS81 3.1 8.9 1.0 CD2 B:HIS26 3.1 6.2 1.0 CD2 B:HIS171 3.2 6.5 1.0 CD2 B:HIS81 3.2 6.7 1.0 OD1 B:ASP167 3.5 7.6 1.0 ND1 B:HIS26 4.2 7.8 1.0 ND1 B:HIS171 4.2 7.8 1.0 ND1 B:HIS81 4.2 8.8 1.0 CG B:HIS26 4.2 7.6 1.0 CG B:HIS81 4.3 7.3 1.0 CG B:HIS171 4.3 5.9 1.0 CB B:ASP167 4.3 5.7 1.0 CZ2 B:TRP128 4.4 7.2 1.0 CB B:TRP169 4.6 5.5 1.0 NE2 B:GLN146 4.7 8.3 1.0 CG B:TRP169 4.8 7.0 1.0 CH2 B:TRP128 4.9 7.6 1.0 CB B:ALA172 4.9 8.6 1.0

R.A.Edwards, M.M.Whittaker, J.W.Whittaker, E.N.Baker, G.B.Jameson. Removing A Hydrogen Bond in the Dimer Interface of Escherichia Coli Manganese Superoxide Dismutase Alters Structure and Reactivity. Biochemistry V. 40 4622 2001.
ISSN: ISSN 0006-2960
PubMed: 11294629
DOI: 10.1021/BI002403H