Magnesium in PDB 6fcd: Human Methionine Adenosyltransferase II Mutant (R264A)

All present enzymatic activity of Human Methionine Adenosyltransferase II Mutant (R264A):
2.5.1.6;

The structure of Human Methionine Adenosyltransferase II Mutant (R264A), PDB code: 6fcd 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)	58.41 / 1.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.141, 94.230, 116.820, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 18.4

The structure of Human Methionine Adenosyltransferase II Mutant (R264A) also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Magnesium atom in the Human Methionine Adenosyltransferase II Mutant (R264A) (pdb code 6fcd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Methionine Adenosyltransferase II Mutant (R264A), PDB code: 6fcd:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human Methionine Adenosyltransferase II Mutant (R264A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Methionine Adenosyltransferase II Mutant (R264A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:32.2 occ:0.75 O31 A:PPV406 2.3 11.5 1.0 O A:HOH540 2.5 24.4 1.0 O A:HOH662 2.5 15.3 1.0 O A:HOH520 2.7 15.0 1.0 P1 A:PPV406 3.8 10.2 1.0 O22 A:PPV406 3.8 14.2 1.0 O A:HOH606 3.9 9.6 1.0 OE2 A:GLU23 3.9 13.2 1.0 OPP A:PPV406 4.3 12.3 1.0 NZ A:LYS181 4.3 10.5 1.0 O11 A:PPV406 4.6 11.2 1.0 OE1 A:GLU23 4.6 12.7 1.0 NZ A:LYS265 4.6 13.9 1.0 O21 A:PPV406 4.7 10.8 1.0 P2 A:PPV406 4.7 11.7 1.0 CD A:GLU23 4.7 14.0 1.0 O A:HOH654 5.0 13.6 1.0

Magnesium binding site 2 out of 2 in the Human Methionine Adenosyltransferase II Mutant (R264A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Methionine Adenosyltransferase II Mutant (R264A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:10.1 occ:1.00 O11 A:PPV406 1.9 11.2 1.0 O A:HOH527 2.0 10.6 1.0 O32 A:PPV406 2.0 12.8 1.0 OD2 A:ASP31 2.1 8.6 1.0 O A:HOH532 2.2 10.0 1.0 O A:HOH654 2.2 13.6 1.0 CG A:ASP31 3.0 8.5 1.0 P2 A:PPV406 3.2 11.7 1.0 P1 A:PPV406 3.2 10.2 1.0 OD1 A:ASP31 3.2 8.7 1.0 OPP A:PPV406 3.4 12.3 1.0 K A:K403 3.7 11.7 0.9 NZ A:LYS265 3.7 13.9 1.0 O22 A:PPV406 3.7 14.2 1.0 O A:HOH631 4.1 29.7 1.0 CE1 A:HIS29 4.1 8.3 1.0 O31 A:PPV406 4.1 11.5 1.0 OD2 A:ASP258 4.2 10.3 0.8 O21 A:PPV406 4.2 10.8 1.0 O A:ALA259 4.3 10.8 1.0 O12 A:PPV406 4.4 15.5 1.0 CB A:ASP31 4.4 8.8 1.0 CB A:ALA264 4.5 8.4 1.0 O A:HOH662 4.5 15.3 1.0 NE2 A:HIS29 4.7 8.2 1.0 O A:ALA264 4.7 9.1 1.0 CE A:LYS265 4.7 12.0 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