Magnesium in PDB 5a19: The Structure of MAT2A in Complex with Ppnp.

All present enzymatic activity of The Structure of MAT2A in Complex with Ppnp.:
2.5.1.6;

The structure of The Structure of MAT2A in Complex with Ppnp., PDB code: 5a19 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)	57.71 / 2.34
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	66.220, 95.490, 117.700, 90.00, 90.00, 90.00
R / Rfree (%)	16.344 / 20.446

The structure of The Structure of MAT2A in Complex with Ppnp. also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Magnesium atom in the The Structure of MAT2A in Complex with Ppnp. (pdb code 5a19). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the The Structure of MAT2A in Complex with Ppnp., PDB code: 5a19:

Magnesium binding site 1 out of 1 in the The Structure of MAT2A in Complex with 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 MAT2A in Complex with Ppnp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg409 b:29.9 occ:1.00 O1G A:PPK403 2.1 26.8 0.8 O A:HOH2012 2.2 29.3 1.0 O2A A:PPK403 2.2 31.1 0.8 O A:HOH2143 2.3 33.5 1.0 O A:HOH2013 2.3 11.6 0.5 OD2 A:ASP31 2.3 22.0 1.0 PA A:PPK403 3.2 34.2 0.8 CG A:ASP31 3.2 21.9 1.0 O4A A:PPK403 3.3 34.6 0.8 PG A:PPK403 3.3 25.4 0.8 OD1 A:ASP31 3.4 21.4 1.0 O3G A:PPK403 3.4 28.5 0.8 NZ A:LYS265 3.7 19.8 1.0 K A:K410 3.8 69.5 1.0 NH2 A:ARG264 3.9 21.8 1.0 O3A A:PPK403 4.2 32.6 0.8 O1A A:PPK403 4.3 31.4 0.8 NE A:ARG264 4.3 20.2 1.0 N3B A:PPK403 4.3 29.0 0.8 OD2 A:ASP258 4.4 42.4 1.0 O A:ALA259 4.4 29.9 1.0 CZ A:ARG264 4.4 20.8 1.0 O2G A:PPK403 4.5 26.1 0.8 CE1 A:HIS29 4.5 21.3 1.0 CB A:ASP31 4.6 21.4 1.0 CB A:ARG264 4.6 19.3 1.0 CE A:LYS265 4.8 19.9 1.0 PB A:PPK403 4.9 35.1 0.8 OD1 A:ASP258 4.9 43.0 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