Magnesium in PDB 7ll3: S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp

All present enzymatic activity of S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp:
2.5.1.6;

The structure of S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp, PDB code: 7ll3 was solved by L.L.Tan, C.J.Jackson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.98 / 2.24
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	123.655, 123.655, 289.409, 90, 90, 120
R / Rfree (%)	21.1 / 23.4

The binding sites of Magnesium atom in the S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp (pdb code 7ll3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp, PDB code: 7ll3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg706 b:87.1 occ:1.00 O B:HOH801 2.5 80.0 1.0 O1B A:PPK705 2.6 110.7 0.7 OE2 B:GLU42 2.8 74.4 1.0 O A:CYS239 3.1 73.0 0.5 O A:CYS239 3.3 72.2 0.5 O2B A:PPK705 3.4 109.0 0.7 CG B:GLU42 3.5 60.8 1.0 CD B:GLU42 3.6 75.1 1.0 PB A:PPK705 3.6 116.8 0.7 CB A:CYS239 3.7 68.4 0.5 O A:HOH802 3.7 69.2 1.0 N A:CYS239 3.8 70.2 0.5 N A:CYS239 3.8 69.7 0.5 CB A:CYS239 3.8 68.7 0.5 C A:CYS239 3.9 67.6 0.5 C A:CYS239 4.0 68.0 0.5 CA A:CYS239 4.0 67.5 0.5 CA A:CYS239 4.0 67.5 0.5 OD1 A:ASP238 4.0 112.1 1.0 OE2 B:GLU55 4.4 122.8 1.0 CG A:ASP238 4.4 97.3 1.0 H3B A:PPK705 4.4 140.0 0.7 N3B A:PPK705 4.5 116.6 0.7 OD2 A:ASP238 4.5 103.8 1.0 C A:ASP238 4.7 75.7 1.0 SG A:CYS239 4.7 69.2 0.5 OE1 B:GLU42 4.8 75.1 1.0 O3A A:PPK705 4.9 109.9 0.7 NH2 A:ARG244 4.9 59.2 1.0 CB B:GLU42 5.0 55.1 1.0 CB B:ALA40 5.0 60.0 1.0

Magnesium binding site 2 out of 2 in the S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of S-Adenosylmethionine Synthetase Co-Crystallized with Uppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg707 b:97.7 occ:1.00 O A:HOH832 2.9 64.0 1.0 O3G A:PPK705 2.9 123.0 0.7 O1A A:PPK705 3.0 90.3 0.7 OE1 A:GLU8 3.1 74.4 1.0 O A:HOH841 3.2 66.6 1.0 NZ A:LYS245 3.6 57.5 1.0 O A:HOH834 3.7 59.6 1.0 OD2 B:ASP271 3.8 86.0 1.0 O2G A:PPK705 3.8 126.0 0.7 PG A:PPK705 4.0 119.1 0.7 CD A:GLU8 4.1 77.7 1.0 OD1 B:ASP271 4.1 86.0 1.0 CE A:LYS245 4.2 66.4 1.0 OE2 A:GLU8 4.3 73.4 1.0 PA A:PPK705 4.3 91.9 0.7 CG B:ASP271 4.4 84.8 1.0 O4A A:PPK705 4.5 102.9 0.7 CA B:GLY260 4.5 70.5 1.0 N B:GLY260 4.7 72.1 1.0 O1G A:PPK705 4.9 107.8 0.7 C B:GLY259 4.9 66.3 1.0 O B:HOH814 4.9 85.9 1.0 CD A:LYS245 4.9 65.7 1.0 O B:GLY259 5.0 77.2 1.0

P.Laurino, C.J.Jackson. S-Adenosylmethionine Synthetase To Be Published.