Magnesium in PDB 7lnn: E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate

All present enzymatic activity of E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate:
2.5.1.6;

The structure of E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate, PDB code: 7lnn 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)	43.63 / 2.50
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	122.336, 122.336, 287.267, 90, 90, 120
R / Rfree (%)	22.2 / 24.3

The binding sites of Magnesium atom in the E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate (pdb code 7lnn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate, PDB code: 7lnn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg705 b:77.0 occ:1.00 O1G A:PPK704 2.0 100.2 1.0 OD2 A:ASP16 2.0 95.7 1.0 O A:HOH801 2.3 81.5 1.0 O A:HOH803 2.6 67.4 1.0 O A:HOH824 2.7 80.2 1.0 O4A A:PPK704 2.7 126.0 1.0 CG A:ASP16 2.9 80.8 1.0 OD1 A:ASP16 3.2 82.9 1.0 PG A:PPK704 3.4 117.2 1.0 O3A A:PPK704 3.6 129.0 1.0 PA A:PPK704 3.6 123.6 1.0 NZ A:LYS245 3.6 59.8 1.0 O2A A:PPK704 3.9 126.7 1.0 NH1 A:ARG244 4.0 77.8 1.0 N3B A:PPK704 4.0 127.6 1.0 O A:CYS239 4.2 72.8 1.0 O3G A:PPK704 4.3 121.9 1.0 CB A:ASP16 4.3 69.9 1.0 O2G A:PPK704 4.3 118.7 1.0 CE1 A:HIS14 4.4 64.1 1.0 PB A:PPK704 4.5 133.4 1.0 CB A:ARG244 4.6 67.9 1.0 OD2 A:ASP238 4.8 117.8 1.0 CE A:LYS245 4.9 60.2 1.0 O1A A:PPK704 5.0 125.8 1.0 OE2 B:GLU42 5.0 78.7 1.0 O A:ARG244 5.0 69.4 1.0

Magnesium binding site 2 out of 2 in the E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli S-Adenosyl Methionine Transferase Co-Crystallized with Guanosine-5'-Imidotriphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg803 b:98.9 occ:1.00 O2G B:PPK802 2.1 102.4 0.8 O B:HOH901 2.2 99.5 1.0 O2A B:PPK802 2.4 141.1 0.8 OD2 B:ASP16 2.4 86.0 1.0 CG B:ASP16 3.2 82.1 1.0 OD1 B:ASP16 3.3 81.6 1.0 PA B:PPK802 3.5 139.8 0.8 PG B:PPK802 3.5 106.0 0.8 O3A B:PPK802 3.8 136.9 0.8 O4A B:PPK802 3.9 140.7 0.8 NZ B:LYS245 4.1 77.0 1.0 O B:CYS239 4.1 88.6 0.5 N3B B:PPK802 4.2 124.8 0.8 NH2 B:ARG244 4.2 78.3 1.0 O B:CYS239 4.3 89.7 0.5 O1G B:PPK802 4.3 111.4 0.8 O3G B:PPK802 4.4 103.4 0.8 CE1 B:HIS14 4.5 87.7 1.0 CB B:ARG244 4.5 76.5 1.0 OE2 A:GLU42 4.5 91.5 1.0 CZ B:ARG244 4.6 71.9 1.0 CB B:ASP16 4.6 74.7 1.0 PB B:PPK802 4.7 135.1 0.8 NE B:ARG244 4.7 75.1 1.0 O1A B:PPK802 4.8 140.4 0.8 O B:ARG244 4.9 77.3 1.0

P.Laurino, C.J.Jackson. Protein and Substrate Flexibility Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferases To Be Published.