Magnesium in PDB 5a1i: The Structure of Human MAT2A in Complex with Sam, Adenosine, Methionine and Ppnp.

All present enzymatic activity of The Structure of Human MAT2A in Complex with Sam, Adenosine, Methionine and Ppnp.:
2.5.1.6;

The structure of The Structure of Human MAT2A in Complex with Sam, Adenosine, Methionine and Ppnp., PDB code: 5a1i 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)	73.37 / 1.09
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.972, 94.074, 117.216, 90.00, 90.00, 90.00
R / Rfree (%)	10.4 / 12.4

The structure of The Structure of Human MAT2A in Complex with Sam, Adenosine, Methionine and Ppnp. also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Magnesium atom in the The Structure of Human MAT2A in Complex with Sam, Adenosine, Methionine and Ppnp. (pdb code 5a1i). 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 Sam, Adenosine, Methionine and Ppnp., PDB code: 5a1i:
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 Sam, Adenosine, Methionine 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 Sam, Adenosine, Methionine and Ppnp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:7.3 occ:0.70 O2G A:PPK400 2.0 7.6 0.6 O1A A:PPK400 2.0 8.8 0.8 O1B A:PPK400 2.0 8.8 0.7 OD2 A:ASP31 2.1 8.7 1.0 O A:HOH1278 2.1 8.8 0.7 O A:HOH1047 2.1 8.6 0.7 CG A:ASP31 3.0 7.7 1.0 PB A:PPK400 3.1 8.4 0.7 OD1 A:ASP31 3.2 8.3 1.0 PG A:PPK400 3.3 11.2 0.6 PA A:PPK400 3.3 8.2 0.8 O A:HOH1581 3.4 18.0 0.3 O3A A:PPK400 3.5 11.3 0.8 N3B A:PPK400 3.5 8.4 0.7 NZ A:LYS265 3.6 9.0 1.0 K A:K403 3.8 11.1 0.7 NH2 A:ARG264 3.9 12.3 1.0 O1G A:PPK400 4.1 11.8 0.6 O2A A:PPK400 4.2 10.5 0.8 CE1 A:HIS29 4.3 8.1 1.0 OD2 A:ASP258 4.3 11.7 0.8 CB A:ASP31 4.3 7.5 1.0 O3G A:PPK400 4.3 11.2 0.6 O4A A:PPK400 4.4 10.1 0.8 O A:ALA259 4.4 10.9 1.0 CB A:ARG264 4.4 7.3 1.0 O2B A:PPK400 4.5 10.4 0.7 NE A:ARG264 4.5 12.3 1.0 CZ A:ARG264 4.5 10.9 1.0 CE A:LYS265 4.7 9.2 1.0 O A:HOH1363 4.8 9.0 0.4 O A:ARG264 4.8 7.4 1.0 O A:HOH1109 4.8 17.7 0.9 NE2 A:HIS29 4.8 8.2 1.0

Magnesium binding site 2 out of 2 in the The Structure of Human MAT2A in Complex with Sam, Adenosine, Methionine 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 Sam, Adenosine, Methionine and Ppnp. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:10.4 occ:0.70 O A:HOH1363 1.6 9.0 0.4 O2A A:PPK400 1.9 10.5 0.8 O A:HOH1310 2.0 13.2 0.7 O A:HOH1330 2.1 9.4 0.7 O A:HOH1279 2.2 12.3 0.8 O1G A:PPK400 2.2 11.8 0.6 O A:HOH1057 2.3 10.7 1.0 PA A:PPK400 3.4 8.2 0.8 PG A:PPK400 3.4 11.2 0.6 N3B A:PPK400 3.6 8.4 0.7 O3A A:PPK400 3.8 11.3 0.8 NZ A:LYS265 3.8 9.0 1.0 OE2 A:GLU23 4.0 9.2 1.0 NZ A:LYS181 4.0 8.4 1.0 O1A A:PPK400 4.1 8.8 0.8 O A:HOH1581 4.2 18.0 0.3 O A:HOH1003 4.2 12.4 1.0 O4A A:PPK400 4.3 10.1 0.8 PB A:PPK400 4.5 8.4 0.7 O2G A:PPK400 4.5 7.6 0.6 CE A:LYS265 4.5 9.2 1.0 O3G A:PPK400 4.5 11.2 0.6 OE1 A:GLU23 4.5 9.8 1.0 CD A:GLU23 4.7 8.8 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