Potassium in PDB 5t30: Human Mnsod-Azide Complex

All present enzymatic activity of Human Mnsod-Azide Complex:
1.15.1.1;

The structure of Human Mnsod-Azide Complex, PDB code: 5t30 was solved by J.Azadmanesh, S.R.Trickel, C.H.Kolar, J.J.Lovelace, G.E.O.Borgstahl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.46 / 1.77
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.900, 77.900, 238.442, 90.00, 90.00, 120.00
R / Rfree (%)	20.9 / 23.9

The structure of Human Mnsod-Azide Complex also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Potassium atom in the Human Mnsod-Azide Complex (pdb code 5t30). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Human Mnsod-Azide Complex, PDB code: 5t30:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Human Mnsod-Azide Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Mnsod-Azide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:K203 b:21.3 occ:1.00 O A:GLY12 2.7 17.0 1.0 O A:HOH359 2.8 19.1 1.0 C A:GLY12 3.6 16.5 1.0 CA A:GLY12 4.3 16.7 1.0 OE1 A:GLU15 4.5 24.9 1.0 N A:ALA13 4.5 16.4 1.0 CA A:ALA13 4.7 16.3 1.0 CB A:GLU15 4.7 18.7 1.0 CG A:GLU15 4.9 20.6 1.0

Potassium binding site 2 out of 2 in the Human Mnsod-Azide Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human Mnsod-Azide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:K204 b:25.9 occ:1.00 O A:HOH441 2.8 30.4 1.0 O A:PRO16 2.9 18.1 1.0 OH A:TYR169 2.9 17.9 1.0 O A:HOH350 3.0 20.7 1.0 NE2 A:GLN168 3.8 20.1 1.0 C A:PRO16 3.8 17.5 1.0 CZ A:TYR169 3.9 17.0 1.0 CE1 A:TYR169 4.1 17.1 1.0 CA A:HIS17 4.3 17.1 1.0 N A:HIS17 4.5 16.6 1.0 CB A:PRO16 4.5 18.1 1.0 O A:HOH438 4.5 23.2 1.0 O A:HIS17 4.6 17.9 1.0 CB A:ALA179 4.7 16.8 1.0 O A:HOH434 4.7 25.0 1.0 O A:HOH339 4.8 18.9 1.0 C A:HIS17 4.8 17.3 1.0 CA A:PRO16 4.8 17.7 1.0 CD A:GLN168 5.0 18.7 1.0

J.Azadmanesh, S.R.Trickel, G.E.O.Borgstahl. Substrate-Analog Binding and Electrostatic Surfaces of Human Manganese Superoxide Dismutase. J. Struct. Biol. V. 199 68 2017.
ISSN: ESSN 1095-8657
PubMed: 28461152
DOI: 10.1016/J.JSB.2017.04.011