Manganese in PDB 1xil: Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine

All present enzymatic activity of Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine:
1.15.1.1;

The structure of Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine, PDB code: 1xil was solved by I.Ayala, J.J.Perry, J.Szczepanski, D.E.Cabelli, J.A.Tainer, M.T.Vala, H.S.Nick, D.N.Silverman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.64 / 1.53
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.696, 75.309, 67.992, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine also contains other interesting chemical elements:

Fluorine

(F)

14 atoms

The binding sites of Manganese atom in the Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine (pdb code 1xil). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine, PDB code: 1xil:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:14.6 occ:1.00 OD1 A:ASP159 2.0 20.8 1.0 O A:HOH685 2.1 21.2 1.0 NE2 A:HIS163 2.1 19.8 1.0 NE2 A:HIS26 2.2 20.0 1.0 NE2 A:HIS74 2.2 21.9 1.0 CG A:ASP159 3.0 18.6 1.0 CD2 A:HIS163 3.1 18.6 1.0 CE1 A:HIS26 3.2 23.0 1.0 CE1 A:HIS74 3.2 21.1 1.0 CE1 A:HIS163 3.2 18.4 1.0 CD2 A:HIS26 3.2 22.2 1.0 CD2 A:HIS74 3.2 21.1 1.0 OD2 A:ASP159 3.4 22.0 1.0 CZ2 A:TRP123 4.2 20.9 1.0 CG A:HIS163 4.3 19.6 1.0 ND1 A:HIS163 4.3 20.7 1.0 ND1 A:HIS26 4.3 23.5 1.0 ND1 A:HIS74 4.3 22.7 1.0 CB A:ASP159 4.3 19.8 1.0 CG A:HIS26 4.3 23.1 1.0 CG A:HIS74 4.3 22.0 1.0 NE2 A:GLN143 4.4 21.8 1.0 CB A:TRP161 4.5 17.6 1.0 CG A:TRP161 4.6 17.4 1.0 CH2 A:TRP123 4.8 22.8 1.0 CD1 A:TRP161 4.8 18.6 1.0 CE2 A:TRP123 5.0 19.8 1.0

Manganese binding site 2 out of 2 in the Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3- Fluorotyrosine within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn600 b:10.8 occ:1.00 OD1 B:ASP159 2.0 16.0 1.0 O B:HOH835 2.1 17.5 1.0 NE2 B:HIS163 2.2 15.7 1.0 NE2 B:HIS26 2.2 15.0 1.0 NE2 B:HIS74 2.2 16.2 1.0 CG B:ASP159 3.0 15.4 1.0 CD2 B:HIS163 3.1 15.8 1.0 CE1 B:HIS74 3.2 15.2 1.0 CE1 B:HIS26 3.2 17.2 1.0 CE1 B:HIS163 3.2 16.3 1.0 CD2 B:HIS74 3.2 15.2 1.0 CD2 B:HIS26 3.2 16.8 1.0 OD2 B:ASP159 3.4 18.0 1.0 CZ2 B:TRP123 4.2 14.6 1.0 ND1 B:HIS163 4.2 18.2 1.0 ND1 B:HIS74 4.3 15.6 1.0 ND1 B:HIS26 4.3 18.4 1.0 CG B:HIS163 4.3 18.1 1.0 CG B:HIS74 4.3 14.8 1.0 CB B:ASP159 4.3 15.3 1.0 CG B:HIS26 4.4 17.4 1.0 NE2 B:GLN143 4.4 16.9 1.0 CB B:TRP161 4.6 15.4 1.0 CG B:TRP161 4.7 15.6 1.0 CD1 B:TRP161 4.8 14.9 1.0 CH2 B:TRP123 4.9 16.4 1.0 CE2 B:TRP123 5.0 14.8 1.0 CB B:ALA164 5.0 17.1 1.0

I.Ayala, J.J.Perry, J.Szczepanski, J.A.Tainer, M.T.Vala, H.S.Nick, D.N.Silverman. Hydrogen Bonding in Human Manganese Superoxide Dismutase Containing 3-Fluorotyrosine Biophys.J. V. 89 4171 2005.
ISSN: ISSN 0006-3495
PubMed: 16150974
DOI: 10.1529/BIOPHYSJ.105.060616