Potassium in PDB 1o92: Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue

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

The structure of Methionine Adenosyltransferase Complexed with Adp and A L-Methionine Analogue, PDB code: 1o92 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 / 3.19
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	115.140, 115.140, 160.450, 90.00, 90.00, 90.00
R / Rfree (%)	24.6 / 26.4

The structure of Methionine Adenosyltransferase Complexed with Adp 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 Adp and A L-Methionine Analogue (pdb code 1o92). 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 Adp and A L-Methionine Analogue, PDB code: 1o92:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Methionine Adenosyltransferase Complexed with Adp 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 Adp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:K1405 b:95.5 occ:1.00 O A:GLY264 3.1 5.1 1.0 CG1 A:ILE267 3.3 10.5 1.0 O B:ARG265 3.4 11.2 1.0 CB A:ILE267 3.5 7.8 1.0 C B:ARG265 3.8 6.2 1.0 CA B:ARG265 4.1 4.6 1.0 CB B:ILE267 4.2 5.4 1.0 CG2 A:ILE267 4.3 7.7 1.0 C A:GLY264 4.3 5.0 1.0 N B:ILE267 4.4 8.3 1.0 O B:GLY264 4.4 13.3 1.0 CA A:ARG265 4.5 7.8 1.0 O A:GLY280 4.5 7.3 1.0 CG B:ARG265 4.6 6.6 1.0 N A:ILE267 4.6 9.5 1.0 CA A:ILE267 4.7 7.0 1.0 N B:LYS266 4.7 6.2 1.0 CD1 A:ILE267 4.7 16.7 1.0 C A:ARG265 4.7 9.4 1.0 CG1 B:ILE267 4.8 8.2 1.0 O A:ARG265 4.9 15.8 1.0 N A:ARG265 4.9 5.6 1.0 CB B:ARG265 4.9 5.4 1.0 CA B:ILE267 5.0 5.9 1.0

Potassium binding site 2 out of 2 in the Methionine Adenosyltransferase Complexed with Adp 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 Adp and A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:K1406 b:81.9 occ:1.00 CB B:ALA282 3.3 6.9 1.0 O B:SER284 3.4 9.0 1.0 O2 B:PO41400 3.7 72.9 1.0 CA B:GLY264 3.9 8.2 1.0 CE B:LYS286 3.9 23.8 1.0 CG2 B:THR263 4.1 2.0 1.0 O3 B:PO41400 4.2 66.9 1.0 O B:THR263 4.2 7.2 1.0 N B:GLY264 4.2 7.4 1.0 C B:THR263 4.3 5.2 1.0 NZ B:LYS286 4.4 25.7 1.0 NH1 A:ARG265 4.5 8.4 1.0 C B:SER284 4.6 4.3 1.0 CA B:ALA282 4.6 3.9 1.0 P B:PO41400 4.6 70.3 1.0 C B:ALA282 4.7 7.6 1.0 CB B:THR263 4.8 2.6 1.0 O B:ALA282 4.9 8.2 1.0 CD B:LYS286 4.9 19.2 1.0 CG B:LYS286 5.0 16.0 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