Manganese in PDB 6elk: C.Elegans Mnsod-3 Mutant - Q142H

All present enzymatic activity of C.Elegans Mnsod-3 Mutant - Q142H:
1.15.1.1;

The structure of C.Elegans Mnsod-3 Mutant - Q142H, PDB code: 6elk was solved by G.J.Hunter, C.H.Trinh, T.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.18 / 1.65
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.530, 81.530, 137.750, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21

The binding sites of Manganese atom in the C.Elegans Mnsod-3 Mutant - Q142H (pdb code 6elk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the C.Elegans Mnsod-3 Mutant - Q142H, PDB code: 6elk:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the C.Elegans Mnsod-3 Mutant - Q142H


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of C.Elegans Mnsod-3 Mutant - Q142H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:18.2 occ:1.00 OD2 A:ASP155 2.0 19.8 1.0 NE2 A:HIS159 2.2 18.8 1.0 O A:HOH372 2.2 19.0 1.0 NE2 A:HIS74 2.2 19.2 1.0 NE2 A:HIS26 2.2 18.3 1.0 CG A:ASP155 3.1 17.0 1.0 CD2 A:HIS159 3.1 19.2 1.0 CE1 A:HIS74 3.1 20.0 1.0 CE1 A:HIS159 3.2 18.9 1.0 CE1 A:HIS26 3.2 19.4 1.0 CD2 A:HIS26 3.2 18.0 1.0 CD2 A:HIS74 3.2 20.3 1.0 OD1 A:ASP155 3.5 16.5 1.0 CZ2 A:TRP122 4.2 21.9 1.0 ND1 A:HIS74 4.3 19.8 1.0 ND1 A:HIS159 4.3 18.0 1.0 CG A:HIS159 4.3 18.3 1.0 ND1 A:HIS26 4.3 19.1 1.0 CG A:HIS74 4.4 20.7 1.0 CG A:HIS26 4.4 19.1 1.0 CB A:ASP155 4.4 18.6 1.0 CB A:TRP157 4.5 16.5 1.0 CG A:TRP157 4.6 16.0 1.0 OH A:TYR34 4.6 27.1 1.0 NE2 A:HIS142 4.7 20.4 1.0 CE2 A:TRP122 4.8 22.6 1.0 NE1 A:TRP122 4.9 23.2 1.0 CD1 A:TRP157 4.9 17.1 1.0

Manganese binding site 2 out of 2 in the C.Elegans Mnsod-3 Mutant - Q142H


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of C.Elegans Mnsod-3 Mutant - Q142H within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn201 b:19.6 occ:1.00 OD2 C:ASP155 2.0 21.1 1.0 O C:HOH393 2.2 19.3 1.0 NE2 C:HIS159 2.2 20.2 1.0 NE2 C:HIS26 2.2 20.2 1.0 NE2 C:HIS74 2.2 20.5 1.0 CG C:ASP155 3.1 20.5 1.0 CE1 C:HIS26 3.1 22.1 1.0 CD2 C:HIS159 3.1 20.3 1.0 CE1 C:HIS74 3.2 20.2 1.0 CE1 C:HIS159 3.2 19.4 1.0 CD2 C:HIS74 3.2 20.6 1.0 CD2 C:HIS26 3.2 21.9 1.0 OD1 C:ASP155 3.6 19.2 1.0 CZ2 C:TRP122 4.2 23.2 1.0 ND1 C:HIS26 4.2 23.0 1.0 ND1 C:HIS74 4.3 19.9 1.0 ND1 C:HIS159 4.3 19.8 1.0 CG C:HIS159 4.3 20.4 1.0 CG C:HIS26 4.3 23.1 1.0 CG C:HIS74 4.3 20.8 1.0 CB C:ASP155 4.3 20.5 1.0 CB C:TRP157 4.5 18.4 1.0 CG C:TRP157 4.6 17.9 1.0 OH C:TYR34 4.7 28.8 1.0 CD1 C:TRP157 4.8 17.5 1.0 NE2 C:HIS142 4.8 20.9 1.0 CE2 C:TRP122 4.8 22.9 1.0 NE1 C:TRP122 4.9 23.9 1.0 CB C:ALA160 5.0 22.8 1.0 CH2 C:TRP122 5.0 23.7 1.0

T.Hunter, R.Bonetta, A.Sacco, M.Vella, P.M.Sultana, C.H.Trinh, H.B.R.Fadia, T.Borowski, R.Garcia-Fandino, T.Stockner, G.J.Hunter. A Single Mutation Is Sufficient to Modify the Metal Selectivity and Specificity of A Eukaryotic Manganese Superoxide Dismutase to Encompass Iron. Chemistry V. 24 5303 2018.
ISSN: ISSN 1521-3765
PubMed: 29178484
DOI: 10.1002/CHEM.201704655