Potassium in PDB 1o90: Methionine Adenosyltransferase Complexed with A L-Methionine Analogue

All present enzymatic activity of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue:
2.5.1.6;

The structure of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue, PDB code: 1o90 was solved by B.Gonzalez, M.A.Pajares, J.A.Hermoso, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 3.10
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	114.890, 114.890, 161.080, 90.00, 90.00, 90.00
R / Rfree (%)	24.4 / 28.6

The structure of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Potassium atom in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue (pdb code 1o90). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue, PDB code: 1o90:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:K1404 b:100.0 occ:1.00 O A:GLY264 3.2 17.5 1.0 O B:ARG265 3.2 22.8 1.0 CG1 A:ILE267 3.4 22.3 1.0 C B:ARG265 3.6 18.3 1.0 CB A:ILE267 3.7 17.8 1.0 CA B:ARG265 3.9 16.0 1.0 N B:ILE267 4.3 17.3 1.0 CB B:ILE267 4.3 14.6 1.0 C A:GLY264 4.4 14.4 1.0 O A:GLY280 4.4 17.3 1.0 O B:GLY264 4.4 24.5 1.0 CG B:ARG265 4.4 16.7 1.0 CG2 A:ILE267 4.4 18.8 1.0 N B:LYS266 4.5 17.9 1.0 CA A:ARG265 4.6 16.0 1.0 CB B:ARG265 4.8 17.4 1.0 N A:ILE267 4.8 21.1 1.0 CD1 A:ILE267 4.8 26.1 1.0 CA A:ILE267 4.9 17.9 1.0 C A:ARG265 4.9 18.6 1.0 CG1 B:ILE267 4.9 21.7 1.0 CA B:ILE267 5.0 15.4 1.0 N A:ARG265 5.0 13.3 1.0 CA B:LYS266 5.0 16.4 1.0

Potassium binding site 2 out of 2 in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:K1405 b:72.8 occ:1.00 O2 B:PO41399 3.1 75.8 1.0 O B:SER284 3.7 16.9 1.0 CE B:LYS286 3.8 30.2 1.0 CB B:ALA282 4.0 14.5 1.0 P B:PO41399 4.2 73.8 1.0 NH1 A:ARG265 4.3 20.4 1.0 O4 B:PO41399 4.4 73.9 1.0 NZ B:LYS286 4.4 33.5 1.0 CG2 B:THR263 4.5 10.2 1.0 O B:THR263 4.5 15.7 1.0 O3 B:PO41399 4.6 74.2 1.0 CA B:GLY264 4.7 17.5 1.0 C B:THR263 4.8 13.4 1.0 CB B:GLU58 4.8 21.3 1.0 CG B:LYS286 4.8 25.1 1.0 N B:GLY264 4.8 15.2 1.0 CD B:LYS286 4.9 26.4 1.0 C B:SER284 4.9 14.1 1.0 CB B:THR263 4.9 10.5 1.0

B.Gonzalez, M.A.Pajares, J.A.Hermoso, D.Guillerm, G.Guillerm, J.Sanz-Aparicio. Crystal Structures of Methionine Adenosyltransferase Complexed with Substrates and Products Reveal the Methionine-Atp Recognition and Give Insights Into the Catalytic Mechanism J.Mol.Biol. V. 331 407 2003.
ISSN: ISSN 0022-2836
PubMed: 12888348
DOI: 10.1016/S0022-2836(03)00728-9