Magnesium in PDB 6hlq: Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp

All present enzymatic activity of Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp:
2.7.7.6;

The structure of Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp also contains other interesting chemical elements:

Zinc

(Zn)

7 atoms

The binding sites of Magnesium atom in the Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp (pdb code 6hlq). 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 Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp, PDB code: 6hlq:

Magnesium binding site 1 out of 1 in the Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Yeast Rna Polymerase I* Elongation Complex Bound to Nucleotide Analog Gmpcpp within 5.0Å range: probe atom residue distance (Å) B Occ R:Mg101 b:18.1 occ:1.00 O3' R:C20 1.7 22.2 1.0 OD1 A:ASP629 1.8 11.0 1.0 OD1 A:ASP627 2.0 10.0 1.0 OD2 A:ASP627 2.4 10.0 1.0 CG A:ASP627 2.5 10.0 1.0 CG A:ASP629 2.8 11.0 1.0 OD2 A:ASP629 3.1 11.0 1.0 C3' R:C20 3.1 22.2 1.0 OD1 A:ASP631 3.3 12.6 1.0 CG A:ASP631 3.8 12.6 1.0 C4' R:C20 3.9 22.2 1.0 CB A:ASP627 3.9 10.0 1.0 OD2 A:ASP631 4.0 12.6 1.0 O2' R:C20 4.0 22.2 1.0 C2' R:C20 4.1 22.2 1.0 C5' T:G2P3000 4.1 40.1 1.0 CB A:ASP629 4.2 11.0 1.0 C4' T:G2P3000 4.2 40.1 1.0 O4' T:G2P3000 4.2 40.1 1.0 N A:ASP629 4.3 11.0 1.0 C5' R:C20 4.3 22.2 1.0 O A:ASP629 4.5 11.0 1.0 C A:ASP629 4.5 11.0 1.0 CA A:ASP629 4.5 11.0 1.0 C A:ASP627 4.6 10.0 1.0 CA A:ASP627 4.6 10.0 1.0 N A:ASP627 4.7 10.0 1.0 O5' R:C20 4.7 22.2 1.0 O A:ASP627 4.8 10.0 1.0 N A:ASP631 4.9 12.6 1.0 N A:PHE628 5.0 7.6 1.0

L.Tafur, Y.Sadian, J.Hanske, R.Wetzel, F.Weis, C.W.Muller. The Cryo-Em Structure of A 12-Subunit Variant of Rna Polymerase I Reveals Dissociation of the A49-A34.5 Heterodimer and Rearrangement of Subunit A12.2. Elife V. 8 2019.
ISSN: ESSN 2050-084X
PubMed: 30913026
DOI: 10.7554/ELIFE.43204