Potassium in PDB 1qm4: 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: 1qm4 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)	10.00 / 2.66
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	115.200, 115.200, 159.980, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 29

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

Magnesium

(Mg)

2 atoms

The binding sites of Potassium atom in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue (pdb code 1qm4). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Methionine Adenosyltransferase Complexed with A L-Methionine Analogue, PDB code: 1qm4:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 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:K406 b:66.2 occ:1.00 O A:GLY264 3.0 19.1 1.0 O B:ARG265 3.3 24.0 1.0 C B:ARG265 3.4 21.9 1.0 CA B:ARG265 3.5 19.6 1.0 O B:GLY264 3.8 19.4 1.0 CG1 A:ILE267 3.9 20.2 1.0 CG B:ARG265 4.0 19.9 1.0 CB A:ILE267 4.0 18.2 1.0 CA A:ARG265 4.1 17.8 1.0 C A:GLY264 4.1 15.2 1.0 CB B:ILE267 4.2 17.1 1.0 N B:LYS266 4.2 21.1 1.0 CB B:ARG265 4.3 17.5 1.0 N B:ILE267 4.4 19.2 1.0 N B:ARG265 4.5 17.6 1.0 C A:ARG265 4.5 18.8 1.0 C B:GLY264 4.6 17.4 1.0 CG2 A:ILE267 4.6 13.1 1.0 O3 A:SO4403 4.6 46.4 1.0 N A:ARG265 4.6 15.6 1.0 CG1 B:ILE267 4.6 21.2 1.0 CG2 B:ILE267 4.8 13.3 1.0 O A:ARG265 4.9 24.3 1.0 CG A:ARG265 4.9 19.1 1.0 O A:GLY280 4.9 24.3 1.0 CA B:LYS266 4.9 17.7 1.0

Potassium binding site 2 out of 3 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 A:K407 b:70.4 occ:1.00 O2 A:SO4403 3.1 36.8 1.0 NH1 B:ARG265 3.8 25.1 1.0 CE A:LYS286 3.9 29.2 1.0 CD B:ARG265 4.1 21.8 1.0 CB A:ALA282 4.1 22.6 1.0 NZ A:LYS286 4.2 37.2 1.0 O A:THR263 4.2 16.1 1.0 CZ B:ARG265 4.2 23.1 1.0 NE B:ARG265 4.3 21.0 1.0 CA A:GLY264 4.4 15.7 1.0 S A:SO4403 4.4 49.6 1.0 O A:SER284 4.5 19.5 1.0 O3 A:SO4403 4.5 46.4 1.0 C A:THR263 4.6 14.8 1.0 N A:GLY264 4.6 16.4 1.0 CG2 A:THR263 4.7 5.4 1.0 O4 A:SO4403 4.8 38.3 1.0 OE2 A:GLU58 5.0 33.7 1.0

Potassium binding site 3 out of 3 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 3 of Methionine Adenosyltransferase Complexed with A L-Methionine Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:K402 b:62.8 occ:1.00 O2 B:SO4401 3.2 34.8 1.0 NH1 A:ARG265 3.7 20.4 1.0 O B:SER284 3.9 18.9 1.0 CE B:LYS286 4.0 28.9 1.0 O B:THR263 4.1 14.4 1.0 CG2 B:THR263 4.1 14.0 1.0 CA B:GLY264 4.3 17.1 1.0 CB B:ALA282 4.3 24.2 1.0 C B:THR263 4.3 15.3 1.0 N B:GLY264 4.4 16.6 1.0 CZ A:ARG265 4.4 22.7 1.0 CB B:THR263 4.5 14.3 1.0 NZ B:LYS286 4.5 33.7 1.0 S B:SO4401 4.5 45.1 1.0 CD A:ARG265 4.6 19.8 1.0 CB B:GLU58 4.7 25.4 1.0 NE A:ARG265 4.8 20.5 1.0 OE2 B:GLU58 4.9 35.8 1.0 CD B:GLU58 5.0 30.3 1.0

B.Gonzalez, M.A.Pajares, J.A.Hermoso, L.Alvarez, F.Garrido, J.R.Sufrin, J.Sanz-Aparicio. The Crystal Structure of Tetrameric Methionine Adenosyltransferase From Rat Liver Reveals the Methionine-Binding Site J.Mol.Biol. V. 300 363 2000.
ISSN: ISSN 0022-2836
PubMed: 10873471
DOI: 10.1006/JMBI.2000.3858