Magnesium in PDB 7r2w: Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine

All present enzymatic activity of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine:
2.5.1.6;

The structure of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine, PDB code: 7r2w was solved by A.Shahar, D.Kleiner, S.Bershtein, R.Zarivach, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.73 / 1.60
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.611, 86.611, 90.982, 90, 90, 90
R / Rfree (%)	18.2 / 22

The structure of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Magnesium atom in the Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine (pdb code 7r2w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine, PDB code: 7r2w:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:61.6 occ:1.00 O2G A:ANP401 2.3 30.9 0.5 O2A A:ANP401 2.3 26.7 0.5 O A:HOH520 2.4 38.2 1.0 O A:HOH579 2.9 33.5 1.0 N3B A:ANP401 3.1 35.3 0.5 PG A:ANP401 3.4 34.9 0.5 PA A:ANP401 3.5 29.2 0.5 O3A A:ANP401 3.9 35.9 0.5 NZ A:LYS246 4.1 26.9 1.0 O3G A:ANP401 4.2 28.7 0.5 PB A:ANP401 4.2 37.0 0.5 O A:HOH588 4.3 25.5 1.0 OE2 A:GLU9 4.3 26.3 1.0 O1A A:ANP401 4.4 33.2 0.5 NZ A:LYS166 4.5 31.7 1.0 O1G A:ANP401 4.5 23.6 0.5 O5' A:ANP401 4.7 31.2 0.5 O1B A:ANP401 4.7 35.7 0.5 CE A:LYS246 4.9 27.9 1.0

Magnesium binding site 2 out of 2 in the Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mutant S-Adenosylmethionine Synthetase From E.Coli Complexed with Amppnp and Methionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:46.3 occ:1.00 O1G A:ANP401 1.8 23.6 0.5 O1A A:ANP401 2.1 33.2 0.5 OD2 A:ASP17 2.2 24.9 1.0 O A:HOH543 2.3 37.0 1.0 O A:HOH541 2.3 42.0 1.0 O2B A:ANP401 2.3 30.4 0.5 PB A:ANP401 2.9 37.0 0.5 PG A:ANP401 3.0 34.9 0.5 CG A:ASP17 3.1 26.6 1.0 N3B A:ANP401 3.2 35.3 0.5 PA A:ANP401 3.2 29.2 0.5 O3A A:ANP401 3.3 35.9 0.5 OD1 A:ASP17 3.3 25.4 1.0 NZ A:LYS246 3.6 26.9 1.0 NH2 A:ARG245 3.8 27.2 1.0 O2G A:ANP401 3.9 30.9 0.5 O2A A:ANP401 4.0 26.7 0.5 O3G A:ANP401 4.2 28.7 0.5 K A:K404 4.2 44.5 1.0 OD2 A:ASP239 4.3 62.1 1.0 CE1 A:HIS15 4.3 26.0 1.0 O1B A:ANP401 4.4 35.7 0.5 CB A:ASP17 4.5 23.6 1.0 O5' A:ANP401 4.5 31.2 0.5 O A:CYS240 4.6 31.9 1.0 CZ A:ARG245 4.6 26.8 1.0 CB A:ARG245 4.6 23.5 1.0 O A:HOH559 4.7 31.6 1.0 NE A:ARG245 4.7 25.9 1.0 O A:ARG245 4.8 24.7 1.0 NE2 A:HIS15 4.9 26.0 1.0 CE A:LYS246 4.9 27.9 1.0

D.Kleiner, Z.Shapiro Tuchman, F.Shmulevich, A.Shahar, R.Zarivach, M.Kosloff, S.Bershtein. Evolution of Homo-Oligomerization of Methionine S-Adenosyltransferases Is Replete with Structure-Function Constrains. Protein Sci. V. 31 E4352 2022.
ISSN: ESSN 1469-896X
PubMed: 35762725
DOI: 10.1002/PRO.4352