Magnesium in PDB 5a1g: The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.

All present enzymatic activity of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.:
2.5.1.6;

The structure of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp., PDB code: 5a1g was solved by B.Murray, S.V.Antonyuk, A.Marina, S.C.Lu, J.M.Mato, S.S.Hasnain, A.L.Rojas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.69 / 1.83
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.390, 94.390, 117.390, 90.00, 90.00, 90.00
R / Rfree (%)	11.982 / 17.49

The structure of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Magnesium atom in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. (pdb code 5a1g). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp., PDB code: 5a1g:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg406 b:18.6 occ:1.00 O2G A:PPK402 2.0 25.5 1.0 O2A A:PPK402 2.0 24.8 1.0 O1B A:PPK402 2.1 20.8 1.0 O A:HOH2015 2.1 24.4 1.0 OD2 A:ASP31 2.1 15.4 1.0 O A:HOH2014 2.2 18.4 1.0 CG A:ASP31 3.0 15.2 1.0 PB A:PPK402 3.1 25.3 1.0 OD1 A:ASP31 3.2 15.5 1.0 PG A:PPK402 3.3 29.9 1.0 PA A:PPK402 3.3 21.3 1.0 O3A A:PPK402 3.5 25.9 1.0 K A:K405 3.7 32.3 1.0 NZ A:LYS265 3.7 17.4 1.0 N3B A:PPK402 3.7 27.3 1.0 NH2 A:ARG264 4.0 19.4 1.0 O1G A:PPK402 4.2 29.6 1.0 O4A A:PPK402 4.2 21.5 1.0 OD2 A:ASP258 4.3 22.4 1.0 CE1 A:HIS29 4.3 17.5 1.0 O1A A:PPK402 4.4 23.9 1.0 CB A:ASP31 4.4 13.7 1.0 O3G A:PPK402 4.4 32.1 1.0 O A:ALA259 4.5 18.7 1.0 NE A:ARG264 4.5 18.0 1.0 O2B A:PPK402 4.5 26.9 1.0 CB A:ARG264 4.5 16.1 1.0 CZ A:ARG264 4.5 18.5 1.0 CE A:LYS265 4.7 15.2 1.0 O A:ARG264 4.8 16.6 1.0 NE2 A:HIS29 4.9 18.8 1.0

Magnesium binding site 2 out of 2 in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg407 b:26.9 occ:0.90 O A:HOH2276 1.9 23.5 0.9 O A:HOH2273 2.0 20.1 1.0 O4A A:PPK402 2.0 21.5 1.0 O1G A:PPK402 2.3 29.6 1.0 O A:HOH2008 2.4 24.6 0.9 O A:HOH2006 2.7 18.9 1.0 N3B A:PPK402 3.1 27.3 1.0 PG A:PPK402 3.3 29.9 1.0 PA A:PPK402 3.4 21.3 1.0 O3A A:PPK402 3.7 25.9 1.0 NZ A:LYS265 4.0 17.4 1.0 PB A:PPK402 4.2 25.3 1.0 O A:HOH2209 4.2 24.5 1.0 O2A A:PPK402 4.2 24.8 1.0 NZ A:LYS181 4.3 15.7 1.0 OE2 A:GLU23 4.3 18.1 1.0 O2G A:PPK402 4.4 25.5 1.0 O1A A:PPK402 4.4 23.9 1.0 O3G A:PPK402 4.4 32.1 1.0 CE A:LYS265 4.7 15.2 1.0 OE1 A:GLU23 4.9 18.7 1.0 O A:HOH2275 5.0 30.7 1.0

B.Murray, S.V.Antonyuk, A.Marina, S.C.Lu, J.M.Mato, S.S.Hasnain, A.L.Rojas. Crystallography Captures Catalytic Steps in Human Methionine Adenosyltransferase Enzymes. Proc.Natl.Acad.Sci.Usa V. 113 2104 2016.
ISSN: ISSN 0027-8424
PubMed: 26858410
DOI: 10.1073/PNAS.1510959113