Potassium in PDB 6fbp: Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form

All present enzymatic activity of Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form:
2.5.1.6;

The structure of Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form, PDB code: 6fbp was solved by J.Panmanee, S.V.Antonyuk, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.08 / 1.65
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.090, 102.871, 108.170, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 19.5

The structure of Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Potassium atom in the Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form (pdb code 6fbp). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form, PDB code: 6fbp:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:K404 b:49.2 occ:1.00 O A:HOH576 2.4 33.3 1.0 O A:HOH662 3.7 30.6 1.0 OD1 A:ASP191 4.1 22.3 1.0 O A:GLN190 4.2 25.3 1.0 CA A:ASP191 4.6 22.3 1.0 CG A:ASP191 4.8 21.7 1.0 CB A:ASP191 4.9 22.9 1.0

Potassium binding site 2 out of 2 in the Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Human Methionine Adenosyltransferase II Mutant (S114A) in P22121 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ B:K405 b:22.5 occ:1.00 O1B B:PPK401 2.7 9.2 0.5 OE2 A:GLU57 2.7 16.9 1.0 OD1 B:ASP258 2.7 20.8 1.0 O B:ALA259 2.7 12.1 1.0 O A:HOH553 2.8 21.1 1.0 O B:HOH527 3.1 20.3 1.0 O B:HOH545 3.2 18.5 1.0 CG B:ASP258 3.6 19.8 1.0 C B:ALA259 3.8 11.2 1.0 CD A:GLU57 3.8 15.4 1.0 O A:HOH663 3.8 22.0 1.0 MG B:MG402 3.9 12.8 0.8 N B:ALA259 3.9 12.7 1.0 OD2 B:ASP258 4.0 22.2 1.0 O B:HOH534 4.1 33.7 1.0 PB B:PPK401 4.1 10.5 0.5 CG A:GLU57 4.1 13.8 1.0 O2B B:PPK401 4.2 10.6 0.5 CA B:ALA259 4.2 12.1 1.0 CB B:ALA259 4.3 11.6 1.0 NH2 B:ARG264 4.5 13.2 1.0 C B:ASP258 4.5 14.0 1.0 O A:HOH555 4.5 29.6 1.0 OE1 A:GLU70 4.8 21.1 1.0 CB B:ASP258 4.8 16.8 1.0 O3A B:PPK401 4.9 10.3 0.5 CA B:ASP258 4.9 15.0 1.0 N B:GLY260 4.9 11.7 1.0 OE1 A:GLU57 4.9 14.5 1.0

J.Panmanee, J.Bradley-Clarke, J.M.Mato, P.M.O'neill, S.V.Antonyuk, S.S.Hasnain. Control and Regulation of S-Adenosylmethionine Biosynthesis By the Regulatory Beta Subunit and Quinolone-Based Compounds. Febs J. V. 286 2135 2019.
ISSN: ISSN 1742-464X
PubMed: 30776190
DOI: 10.1111/FEBS.14790