Magnesium in PDB 8qqi: E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800

All present enzymatic activity of E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800:
5.6.2.2;

The binding sites of Magnesium atom in the E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800 (pdb code 8qqi). 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 Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800, PDB code: 8qqi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg901 b:27.5 occ:1.00 OE2 B:GLU424 2.4 23.7 1.0 OD2 B:ASP498 3.2 18.6 1.0 CD B:GLU424 3.3 19.1 1.0 OE1 B:GLU424 3.8 16.5 1.0 CG B:ASP498 4.0 19.4 1.0 OP1 E:DA12 4.1 20.0 1.0 OD2 B:ASP500 4.2 19.5 1.0 O3' E:DA11 4.3 14.1 1.0 CB B:ASP498 4.3 12.5 1.0 CG B:GLU424 4.4 15.1 1.0 OH C:TYR122 4.7 27.3 1.0 CB B:ASP502 4.9 11.6 1.0 P E:DA12 4.9 20.0 1.0

Magnesium binding site 2 out of 2 in the E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E.Coli Dna Gyrase in Complex with 217 Bp Substrate Dna and Lei-800 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg901 b:27.5 occ:1.00 OE2 D:GLU424 2.4 23.7 1.0 OD2 D:ASP498 3.2 18.6 1.0 CD D:GLU424 3.3 19.1 1.0 OE1 D:GLU424 3.8 16.5 1.0 OP1 F:DG12 3.9 20.0 1.0 O3' F:DT11 4.0 20.0 1.0 CG D:ASP498 4.0 19.4 1.0 OD2 D:ASP500 4.2 19.5 1.0 CB D:ASP498 4.3 12.5 1.0 CG D:GLU424 4.4 15.1 1.0 P F:DG12 4.7 20.0 1.0 OH A:TYR122 4.7 27.3 1.0 CB D:ASP502 4.9 11.6 1.0

D.Ghilarov, N.I.Martin, M.Van Der Stelt. Discovery of Isoquinoline Sulfonamides As Gyrase Inhibitors Active Against Fluoroquinolone-Resistant Bacteria To Be Published.