Potassium in PDB 1o93: Methionine Adenosyltransferase Complexed with Atp and A L-Methionine Analogue

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

The structure of Methionine Adenosyltransferase Complexed with Atp and A L-Methionine Analogue, PDB code: 1o93 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 / 3.49
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	115.200, 115.200, 160.890, 90.00, 90.00, 90.00
R / Rfree (%)	22.4 / 27.3

The structure of Methionine Adenosyltransferase Complexed with Atp and 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 Atp and A L-Methionine Analogue (pdb code 1o93). 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 Atp and A L-Methionine Analogue, PDB code: 1o93:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Methionine Adenosyltransferase Complexed with Atp and 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 Atp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:K1404 b:20.0 occ:1.00 O A:GLY264 2.8 8.4 1.0 O B:ARG265 3.1 4.5 1.0 CG1 A:ILE267 3.5 9.9 1.0 C B:ARG265 3.5 2.5 1.0 CA B:ARG265 3.7 2.5 1.0 CB A:ILE267 3.9 7.7 1.0 C A:GLY264 4.0 6.8 1.0 CG B:ARG265 4.1 2.0 1.0 CA A:ARG265 4.3 5.1 1.0 O B:GLY264 4.3 11.1 1.0 CB B:ARG265 4.5 2.2 1.0 N B:LYS266 4.5 4.4 1.0 N B:ILE267 4.5 4.7 1.0 CB B:ILE267 4.6 3.6 1.0 O A:GLY280 4.6 5.2 1.0 N A:ARG265 4.6 3.9 1.0 C A:ARG265 4.7 6.0 1.0 CG2 A:ILE267 4.7 2.0 1.0 CD B:ARG265 4.8 6.2 1.0 N A:ILE267 4.8 6.5 1.0 N B:ARG265 4.9 4.6 1.0 CD1 A:ILE267 4.9 12.8 1.0 O A:ARG265 5.0 10.6 1.0 C B:GLY264 5.0 7.3 1.0

Potassium binding site 2 out of 2 in the Methionine Adenosyltransferase Complexed with Atp and 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 Atp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:K1405 b:20.0 occ:1.00 O B:SER284 3.5 13.3 1.0 CB B:ALA282 3.7 8.1 1.0 CE B:LYS286 3.9 25.4 1.0 CG2 B:THR263 4.3 3.9 1.0 O B:THR263 4.3 6.2 1.0 NH1 A:ARG265 4.3 4.6 1.0 CA B:GLY264 4.3 8.4 1.0 O3 B:PO41399 4.3 20.0 1.0 NZ B:LYS286 4.5 27.9 1.0 C B:THR263 4.5 5.0 1.0 N B:GLY264 4.5 6.1 1.0 C B:SER284 4.8 10.0 1.0 CB B:THR263 4.8 7.4 1.0 CD B:LYS286 4.9 23.4 1.0 CG B:LYS286 4.9 21.2 1.0 P B:PO41399 4.9 20.0 1.0 O4 B:PO41399 4.9 20.0 1.0 CB B:GLU58 4.9 22.6 1.0 O2 B:PO41399 4.9 20.0 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