Magnesium in PDB 7ae1: Cryo-Em Structure of Human Rna Polymerase III Elongation Complex 1

All present enzymatic activity of Cryo-Em Structure of Human Rna Polymerase III Elongation Complex 1:
2.7.7.6;

The structure of Cryo-Em Structure of Human Rna Polymerase III Elongation Complex 1 also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Zinc	(Zn)	7 atoms

The binding sites of Magnesium atom in the Cryo-Em Structure of Human Rna Polymerase III Elongation Complex 1 (pdb code 7ae1). 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 Cryo-Em Structure of Human Rna Polymerase III Elongation Complex 1, PDB code: 7ae1:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Human Rna Polymerase III Elongation Complex 1


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 Human Rna Polymerase III Elongation Complex 1 within 5.0Å range: probe atom residue distance (Å) B Occ R:Mg101 b:47.7 occ:1.00 O3' R:G19 1.6 84.1 1.0 OD1 A:ASP501 1.9 51.5 1.0 OD1 A:ASP499 2.3 50.8 1.0 OD2 A:ASP499 2.7 50.8 1.0 CG A:ASP499 2.8 50.8 1.0 CG A:ASP501 2.8 51.5 1.0 C3' R:G19 2.9 84.1 1.0 OD2 A:ASP501 3.1 51.5 1.0 OD1 A:ASP503 3.2 54.2 1.0 C4' R:G19 3.3 84.1 1.0 O2' R:G19 3.6 84.1 1.0 C2' R:G19 3.8 84.1 1.0 CB A:ASP503 3.8 54.2 1.0 C5' R:G19 3.9 84.1 1.0 CG A:ASP503 3.9 54.2 1.0 CB A:ASP501 4.2 51.5 1.0 CB A:ASP499 4.3 50.8 1.0 N A:ASP501 4.3 51.5 1.0 CA A:ASP503 4.4 54.2 1.0 N A:ASP503 4.4 54.2 1.0 O A:ASP501 4.6 51.5 1.0 CA A:ASP501 4.6 51.5 1.0 O5' R:G19 4.6 84.1 1.0 C A:ASP501 4.6 51.5 1.0 O4' R:G19 4.7 84.1 1.0 N A:ASP499 4.7 50.8 1.0 NH2 A:ARG464 4.7 51.9 1.0 CA A:ASP499 4.9 50.8 1.0 C A:ASP499 4.9 50.8 1.0 C1' R:G19 4.9 84.1 1.0 N A:PHE500 5.0 44.0 1.0

M.Girbig, A.D.Misiaszek, M.K.Vorlaender, A.Lafita, H.Groetsch, F.Baudin, A.Bateman, C.W.Mueller. Cryo-Em Structures of Human Rna Polymerase III in Its Unbound and Transcribing States To Be Published.
DOI: 10.1038/S41594-020-00555-5