Potassium in PDB 8ssc: Full-Length Methionine Synthase From Thermus Thermophilus HB8

All present enzymatic activity of Full-Length Methionine Synthase From Thermus Thermophilus HB8:
2.1.1.13;

The structure of Full-Length Methionine Synthase From Thermus Thermophilus HB8, PDB code: 8ssc was solved by K.Yamada, J.Mendoza, M.Koutmos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	106.64 / 2.75
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	134.804, 134.804, 174.738, 90, 90, 90
R / Rfree (%)	20.2 / 25.3

The binding sites of Potassium atom in the Full-Length Methionine Synthase From Thermus Thermophilus HB8 (pdb code 8ssc). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Full-Length Methionine Synthase From Thermus Thermophilus HB8, PDB code: 8ssc:

Potassium binding site 1 out of 1 in the Full-Length Methionine Synthase From Thermus Thermophilus HB8


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Full-Length Methionine Synthase From Thermus Thermophilus HB8 within 5.0Å range: probe atom residue distance (Å) B Occ A:K2000 b:97.3 occ:1.00 O A:HOH2137 2.7 58.6 1.0 OD1 A:ASP53 2.8 69.0 1.0 O A:ASP53 2.9 50.9 1.0 O A:GLY321 2.9 67.2 1.0 O A:GLY54 3.0 55.4 1.0 OE2 A:GLU106 3.0 73.0 1.0 C A:ASP53 3.4 51.6 1.0 CD A:GLU106 3.5 68.2 1.0 C A:GLY54 3.5 50.5 1.0 O A:HOH2171 3.6 67.3 1.0 CD2 A:LEU281 3.7 55.0 1.0 CA A:GLY54 3.7 54.5 1.0 OE1 A:GLU106 3.7 78.0 1.0 CG A:ASP53 3.8 67.6 1.0 N A:GLY54 3.8 54.9 1.0 C A:GLY321 4.1 51.7 1.0 CG A:GLU106 4.3 57.7 1.0 N A:ALA55 4.4 55.0 1.0 CA A:ASP53 4.4 52.3 1.0 O A:HOH2102 4.6 58.8 1.0 OD2 A:ASP53 4.6 74.7 1.0 CB A:ASP53 4.6 53.6 1.0 N A:ASP53 4.7 51.4 1.0 N A:GLY321 4.8 54.3 1.0 OE2 A:GLU191 4.9 104.5 1.0 CA A:ALA55 4.9 56.3 1.0

J.Mendoza, M.K.Purchal, K.Yamada, M.Koutmos. Structure of Full-Length Cobalamin-Dependent Methionine Synthase and Cofactor Loading Captured in Crystallo To Be Published.
DOI: 10.1038/S41467-023-42037-4