Magnesium in PDB 8qn8: Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II

All present enzymatic activity of Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II:
2.7.7.6;

The structure of Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II (pdb code 8qn8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II, PDB code: 8qn8:

Magnesium binding site 1 out of 1 in the Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State II within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg2003 b:12.9 occ:1.00 OD1 D:ASP535 2.0 13.3 1.0 OD1 D:ASP539 2.1 16.1 1.0 OD1 D:ASP537 2.2 15.8 1.0 OD2 H:ASP483 2.4 19.3 1.0 CG D:ASP535 2.8 13.3 1.0 OD2 D:ASP535 2.9 13.3 1.0 CG D:ASP539 2.9 16.1 1.0 CG D:ASP537 3.1 15.8 1.0 OD2 D:ASP539 3.1 16.1 1.0 OD2 D:ASP537 3.3 15.8 1.0 CG H:ASP483 3.4 19.3 1.0 OD1 H:ASP482 3.5 20.0 1.0 CB H:ASP483 3.6 19.3 1.0 O D:ASP535 3.8 13.3 1.0 N H:ASP483 4.1 19.3 1.0 CB D:ASP535 4.2 13.3 1.0 CB D:ASP539 4.3 16.1 1.0 OD1 H:ASP483 4.5 19.3 1.0 CB D:ASP537 4.5 15.8 1.0 CA H:ASP483 4.5 19.3 1.0 C D:ASP535 4.6 13.3 1.0 N D:ASP539 4.6 16.1 1.0 N D:ASP535 4.6 13.3 1.0 CG H:ASP482 4.6 20.0 1.0 CA D:ASP535 4.7 13.3 1.0 N D:ASP537 4.8 15.8 1.0 CA D:ASP539 4.8 16.1 1.0 C D:ASP537 4.9 15.8 1.0 CA D:ASP537 5.0 15.8 1.0

T.Koval, L.Dohnalek, K.Libor, T.Kouba. Molecular Insights Into Rna Polymerase Recycling By Mycobacterial Held To Be Published.