Magnesium in PDB 1i3q: Rna Polymerase II Crystal Form I at 3.1 A Resolution

All present enzymatic activity of Rna Polymerase II Crystal Form I at 3.1 A Resolution:
2.7.7.6;

The structure of Rna Polymerase II Crystal Form I at 3.1 A Resolution, PDB code: 1i3q was solved by P.Cramer, D.A.Bushnell, R.D.Kornberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 3.10
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	130.700, 224.800, 369.400, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 28.3

The structure of Rna Polymerase II Crystal Form I at 3.1 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Magnesium atom in the Rna Polymerase II Crystal Form I at 3.1 A Resolution (pdb code 1i3q). 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 Rna Polymerase II Crystal Form I at 3.1 A Resolution, PDB code: 1i3q:

Magnesium binding site 1 out of 1 in the Rna Polymerase II Crystal Form I at 3.1 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rna Polymerase II Crystal Form I at 3.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg3001 b:58.4 occ:1.00 OD1 A:ASP481 1.9 75.3 1.0 OD2 A:ASP483 2.2 53.0 1.0 OD1 A:ASP485 2.5 61.1 1.0 OD2 A:ASP485 2.5 53.9 1.0 CG A:ASP485 2.7 56.8 1.0 CG A:ASP481 3.0 73.1 1.0 CG A:ASP483 3.1 55.7 1.0 OD1 A:ASP483 3.4 59.8 1.0 OD2 A:ASP481 3.4 79.1 1.0 CB A:ASP485 4.2 49.8 1.0 CB A:ASP481 4.2 63.6 1.0 CB A:ASP483 4.5 52.8 1.0 N A:ASP485 4.6 42.4 1.0 O A:ASP481 4.6 53.4 1.0 N A:ASP483 4.6 47.5 1.0 N A:ASP481 4.6 52.1 1.0 CA A:ASP485 4.7 42.1 1.0 C A:ASP481 4.7 55.0 1.0 CA A:ASP481 4.8 56.7 1.0 CA A:ASP483 5.0 48.8 1.0

P.Cramer, D.A.Bushnell, R.D.Kornberg. Structural Basis of Transcription: Rna Polymerase II at 2.8 Angstrom Resolution. Science V. 292 1863 2001.
ISSN: ISSN 0036-8075
PubMed: 11313498
DOI: 10.1126/SCIENCE.1059493