Magnesium in PDB 8q3i: Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State I

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

The structure of Mycobacterium Smegmatis Rna Polymerase in Complex with Held, Siga and Rbpa in State I 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 I (pdb code 8q3i). 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 I, PDB code: 8q3i:

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


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 I within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg2003 b:16.0 occ:1.00 OD2 D:ASP537 2.2 13.9 1.0 OD1 D:ASP535 2.5 13.4 1.0 OD1 D:ASP537 2.6 13.9 1.0 OD1 D:ASP539 2.6 16.1 1.0 CG D:ASP537 2.7 13.9 1.0 OD2 D:ASP539 3.0 16.1 1.0 CG D:ASP539 3.0 16.1 1.0 CG D:ASP535 3.4 13.4 1.0 OD2 D:ASP535 3.6 13.4 1.0 H D:ASP537 3.8 13.9 1.0 H D:ASP539 3.9 16.1 1.0 CB D:ASP537 4.1 13.9 1.0 O D:ASP535 4.3 13.4 1.0 CB D:ASP539 4.3 16.1 1.0 H D:ASP535 4.4 13.4 1.0 N D:ASP539 4.4 16.1 1.0 HH21 D:ARG500 4.5 13.8 1.0 HB2 D:ASP537 4.5 13.9 1.0 N D:ASP537 4.5 13.9 1.0 HB2 D:ASP539 4.6 16.1 1.0 H D:GLY538 4.7 13.9 1.0 HA D:ASP539 4.7 16.1 1.0 CA D:ASP537 4.7 13.9 1.0 HB3 D:ASP537 4.7 13.9 1.0 CB D:ASP535 4.7 13.4 1.0 N D:GLY538 4.7 13.9 1.0 C D:ASP535 4.7 13.4 1.0 CA D:ASP539 4.7 16.1 1.0 C D:ASP537 4.7 13.9 1.0 N D:ASP535 5.0 13.4 1.0

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