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Manganese in PDB 5n56: Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda

Enzymatic activity of Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda

All present enzymatic activity of Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda:
1.15.1.1;

Protein crystallography data

The structure of Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda, PDB code: 5n56 was solved by A.Barwinska-Sendra, A.Basle, K.Waldron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.30 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.275, 68.356, 56.724, 90.00, 99.45, 90.00
R / Rfree (%) 15 / 23.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda (pdb code 5n56). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda, PDB code: 5n56:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 5n56

Go back to Manganese Binding Sites List in 5n56
Manganese binding site 1 out of 2 in the Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:25.6
occ:1.00
OD2 A:ASP161 2.1 24.2 1.0
NE2 A:HIS81 2.1 28.4 1.0
O A:HOH320 2.2 25.1 1.0
NE2 A:HIS27 2.4 27.4 1.0
NE2 A:HIS165 2.4 31.1 1.0
CG A:ASP161 3.1 28.9 1.0
CE1 A:HIS81 3.1 29.9 1.0
CD2 A:HIS81 3.1 30.7 1.0
CD2 A:HIS165 3.3 33.4 1.0
CD2 A:HIS27 3.3 28.8 1.0
CE1 A:HIS27 3.3 28.1 1.0
OD1 A:ASP161 3.4 25.5 1.0
CE1 A:HIS165 3.4 27.5 1.0
ND1 A:HIS81 4.2 30.4 1.0
CG A:HIS81 4.2 29.4 1.0
CZ2 A:TRP128 4.3 27.2 1.0
CB A:ASP161 4.3 23.9 1.0
ND1 A:HIS27 4.4 29.5 1.0
CG A:HIS27 4.5 28.1 1.0
CG A:HIS165 4.5 31.5 1.0
ND1 A:HIS165 4.5 31.3 1.0
NE2 A:GLN146 4.6 30.9 1.0
CB A:TRP163 4.6 22.2 1.0
CG A:TRP163 4.8 24.0 1.0
CH2 A:TRP128 4.9 29.5 1.0
CE2 A:TYR35 4.9 37.1 1.0
CD1 A:TRP163 5.0 24.9 1.0

Manganese binding site 2 out of 2 in 5n56

Go back to Manganese Binding Sites List in 5n56
Manganese binding site 2 out of 2 in the Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Staphylococcus Aureus Mn-Dependent Superoxide Dismutase Soda within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn201

b:29.0
occ:1.00
OD2 B:ASP161 2.1 23.0 1.0
NE2 B:HIS81 2.2 20.5 1.0
NE2 B:HIS165 2.2 27.9 1.0
O B:HOH336 2.2 30.9 1.0
NE2 B:HIS27 2.4 26.1 1.0
CE1 B:HIS81 3.1 19.3 1.0
CG B:ASP161 3.1 20.6 1.0
CD2 B:HIS165 3.1 25.4 1.0
CD2 B:HIS81 3.2 18.2 1.0
CE1 B:HIS165 3.2 23.6 1.0
CE1 B:HIS27 3.3 21.9 1.0
CD2 B:HIS27 3.3 24.4 1.0
OD1 B:ASP161 3.5 21.6 1.0
ND1 B:HIS81 4.2 20.8 1.0
CG B:HIS165 4.3 24.3 1.0
ND1 B:HIS165 4.3 27.1 1.0
CG B:HIS81 4.3 20.5 1.0
CZ2 B:TRP128 4.4 21.0 1.0
CB B:ASP161 4.4 18.3 1.0
ND1 B:HIS27 4.4 24.5 1.0
CG B:HIS27 4.5 20.4 1.0
CB B:TRP163 4.5 17.3 1.0
NE2 B:GLN146 4.6 26.3 1.0
CG B:TRP163 4.7 18.1 1.0
CH2 B:TRP128 5.0 24.8 1.0

Reference:

A.Barwinska-Sendra, A.Basle, K.J.Waldron, S.Un. A Charge Polarization Model For the Metal-Specific Activity of Superoxide Dismutases. Phys Chem Chem Phys V. 20 2363 2018.
ISSN: ESSN 1463-9084
PubMed: 29308487
DOI: 10.1039/C7CP06829H
Page generated: Sat Aug 16 18:36:25 2025

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