Magnesium in PDB 9ex7: Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr

All present enzymatic activity of Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr:
2.1.1.72;

The binding sites of Magnesium atom in the Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr (pdb code 9ex7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr, PDB code: 9ex7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1301 b:81.8 occ:1.00 OD2 B:ASP999 2.0 113.5 1.0 OD1 B:ASP999 2.0 117.5 1.0 OD2 B:ASP997 2.1 120.3 1.0 CG B:ASP999 2.3 114.0 1.0 O B:ILE1001 2.5 102.0 1.0 OD2 B:ASP1012 2.8 138.3 1.0 CG B:ASP997 2.9 117.0 1.0 OD1 B:ASP997 2.9 121.8 1.0 OH B:TYR1113 3.0 123.0 1.0 CG B:ASP1012 3.6 142.8 1.0 C B:ILE1001 3.6 97.5 1.0 CB B:ASP999 3.8 109.8 1.0 N B:ILE1001 3.9 104.8 1.0 CB B:ASP1012 4.2 140.0 1.0 CZ B:TYR1113 4.2 120.4 1.0 CA B:ILE1001 4.3 94.1 1.0 CB B:ASP997 4.3 109.5 1.0 OD1 B:ASP1012 4.4 146.3 1.0 N B:GLY1000 4.5 107.5 1.0 N B:ASP999 4.5 112.7 1.0 CB B:ILE1001 4.6 90.7 1.0 CA B:ASP999 4.6 109.0 1.0 N B:LEU1002 4.7 98.2 1.0 CD2 B:LEU1002 4.8 103.8 1.0 CD B:PRO1003 4.8 106.6 1.0 CE2 B:TYR1113 4.8 118.8 1.0 C B:ASP999 4.9 110.2 1.0 CA B:LEU1002 5.0 97.8 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of the E. Coli Brxx Methyltransferase in Complex with Ocr within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1301 b:39.4 occ:1.00 OD2 A:ASP999 1.9 59.2 1.0 OD1 A:ASP999 2.0 65.6 1.0 OD2 A:ASP997 2.1 75.9 1.0 CG A:ASP999 2.2 66.5 1.0 O A:ILE1001 2.5 53.4 1.0 CG A:ASP997 2.8 66.2 1.0 OD1 A:ASP997 2.9 73.5 1.0 OH A:TYR1113 2.9 81.0 1.0 OD2 A:ASP1012 3.1 89.9 1.0 C A:ILE1001 3.7 52.2 1.0 CB A:ASP999 3.7 71.8 1.0 CG A:ASP1012 3.8 89.0 1.0 N A:ILE1001 4.0 72.8 1.0 CZ A:TYR1113 4.2 79.1 1.0 CB A:ASP997 4.3 54.2 1.0 CA A:ILE1001 4.3 55.8 1.0 N A:GLY1000 4.4 72.6 1.0 CB A:ASP1012 4.5 80.9 1.0 N A:ASP999 4.5 66.3 1.0 OD1 A:ASP1012 4.5 94.9 1.0 CA A:ASP999 4.6 66.0 1.0 CB A:ILE1001 4.7 54.4 1.0 N A:LEU1002 4.7 63.5 1.0 CD2 A:LEU1002 4.7 63.2 1.0 CD A:PRO1003 4.8 62.7 1.0 CE1 A:TYR1113 4.8 76.6 1.0 C A:ASP999 4.9 64.6 1.0 CA A:LEU1002 4.9 60.5 1.0 C A:GLY1000 5.0 73.5 1.0

A.Drobiazko, M.C.Adams, M.Skutel, K.Potekhina, O.Kotovskaya, A.Trofimova, M.Matlashov, D.Yatselenko, K.L.Maxwell, T.R.Blower, K.Severinov, D.Ghilarov, A.Isaev. Molecular Basis of Foreign Dna Recognition By Brex Anti-Phage Immunity System. Nat Commun V. 16 1825 2025.
ISSN: ESSN 2041-1723
PubMed: 39979294
DOI: 10.1038/S41467-025-57006-2