Magnesium in PDB 4ay7: Methyltransferase From Methanosarcina Mazei

All present enzymatic activity of Methyltransferase From Methanosarcina Mazei:
2.1.1.247;

The structure of Methyltransferase From Methanosarcina Mazei, PDB code: 4ay7 was solved by A.Hoeppner, F.Thomas, A.Rueppel, R.Hensel, W.Blankenfeldt, P.Bayer, A.Faust, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.71 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.209, 167.419, 45.849, 90.00, 117.36, 90.00
R / Rfree (%)	16.304 / 21.287

The structure of Methyltransferase From Methanosarcina Mazei also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Methyltransferase From Methanosarcina Mazei (pdb code 4ay7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Methyltransferase From Methanosarcina Mazei, PDB code: 4ay7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Methyltransferase From Methanosarcina Mazei


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methyltransferase From Methanosarcina Mazei within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg600 b:44.3 occ:1.00 O A:HOH2201 2.0 44.8 1.0 O A:HOH2199 2.1 26.7 1.0 OD1 A:ASP313 2.2 21.0 1.0 CG A:ASP313 3.4 20.1 1.0 NZ A:LYS273 3.7 25.6 1.0 O A:HOH2013 3.8 32.0 1.0 O A:GLY311 4.1 19.2 1.0 OD2 A:ASP313 4.1 19.7 1.0 O A:HOH2018 4.2 42.0 1.0 CB A:ASP313 4.4 19.2 1.0 CE A:LYS273 4.4 24.2 1.0 O A:HOH2012 4.6 34.5 1.0 O A:HOH2200 4.7 24.0 1.0 CA A:ASP313 4.7 18.2 1.0

Magnesium binding site 2 out of 2 in the Methyltransferase From Methanosarcina Mazei


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Methyltransferase From Methanosarcina Mazei within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg600 b:36.2 occ:1.00 O B:HOH2184 2.0 49.4 1.0 O B:HOH2182 2.1 26.1 1.0 OD1 B:ASP313 2.2 21.9 1.0 O B:HOH2185 2.2 26.7 1.0 CG B:ASP313 3.5 21.7 1.0 O B:HOH2010 3.6 33.4 1.0 NZ B:LYS273 3.8 26.1 1.0 OD2 B:ASP313 4.1 20.7 1.0 O B:GLY311 4.2 22.2 1.0 O B:HOH2013 4.3 32.3 1.0 CB B:ASP313 4.5 20.4 1.0 CE B:LYS273 4.6 24.9 1.0 CA B:ASP313 4.7 20.0 1.0 O B:HOH2183 4.7 26.8 1.0

A.Hoeppner, F.Thomas, A.Rueppel, R.Hensel, W.Blankenfeldt, P.Bayer, A.Faust. Structure of the Corrinoid:Coenzyme M Methyltransferase Mtaa From Methanosarcina Mazei Acta Crystallogr.,Sect.D V. 68 1549 2012.
ISSN: ISSN 0907-4449
PubMed: 23090404
DOI: 10.1107/S090744491203853X