Potassium in PDB 1o9t: Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine

All present enzymatic activity of Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine:
2.5.1.6;

The structure of Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine, PDB code: 1o9t 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 / 2.9
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	114.990, 114.990, 160.340, 90.00, 90.00, 90.00
R / Rfree (%)	26.5 / 28.8

The structure of Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Potassium atom in the Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine (pdb code 1o9t). 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 Both Substrates Atp and Methionine, PDB code: 1o9t:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine


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 Both Substrates Atp and Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:K1402 b:99.0 occ:1.00 O A:GLY264 2.7 18.8 1.0 O B:ARG265 3.1 27.1 1.0 CG1 A:ILE267 3.5 27.4 1.0 C B:ARG265 3.6 21.8 1.0 CA B:ARG265 3.7 18.4 1.0 CB A:ILE267 3.8 25.0 1.0 C A:GLY264 3.9 16.6 1.0 CG B:ARG265 4.0 20.8 1.0 CA A:ARG265 4.1 19.4 1.0 O B:GLY264 4.3 26.0 1.0 CB B:ARG265 4.4 18.1 1.0 N A:ARG265 4.5 17.0 1.0 C A:ARG265 4.5 22.8 1.0 N B:LYS266 4.6 22.2 1.0 CD B:ARG265 4.6 23.1 1.0 O A:GLY280 4.7 20.9 1.0 N B:ILE267 4.7 25.4 1.0 CB B:ILE267 4.7 22.5 1.0 N A:ILE267 4.8 24.5 1.0 CG2 A:ILE267 4.8 25.6 1.0 O A:ARG265 4.8 27.9 1.0 CD1 A:ILE267 4.9 31.7 1.0 N B:ARG265 4.9 20.3 1.0 CA A:ILE267 4.9 22.6 1.0

Potassium binding site 2 out of 2 in the Methionine Adenosyltransferase Complexed with Both Substrates Atp and Methionine


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 Both Substrates Atp and Methionine within 5.0Å range: probe atom residue distance (Å) B Occ B:K1399 b:74.8 occ:1.00 O B:SER284 3.5 23.8 1.0 O1 B:PO41398 3.9 89.3 1.0 CB B:ALA282 3.9 22.7 1.0 CE B:LYS286 3.9 26.4 1.0 CG2 B:THR263 4.2 12.0 1.0 O B:THR263 4.3 20.2 1.0 CA B:GLY264 4.4 19.8 1.0 NH1 A:ARG265 4.4 21.7 1.0 C B:THR263 4.5 19.6 1.0 N B:GLY264 4.6 20.7 1.0 NZ B:LYS286 4.6 28.7 1.0 CB B:THR263 4.7 15.1 1.0 CB B:GLU58 4.7 27.0 1.0 C B:SER284 4.7 22.0 1.0 CG B:LYS286 5.0 28.1 1.0 O B:CYS57 5.0 29.4 1.0 CD B:LYS286 5.0 27.4 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