Magnesium in PDB 1sfo: Rna Polymerase II Strand Separated Elongation Complex

All present enzymatic activity of Rna Polymerase II Strand Separated Elongation Complex:
2.7.7.6;

The structure of Rna Polymerase II Strand Separated Elongation Complex, PDB code: 1sfo was solved by K.D.Westover, 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)	39.86 / 3.61
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	167.076, 221.256, 193.685, 90.00, 100.10, 90.00
R / Rfree (%)	31.5 / 34.3

The structure of Rna Polymerase II Strand Separated Elongation Complex also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Magnesium atom in the Rna Polymerase II Strand Separated Elongation Complex (pdb code 1sfo). 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 Strand Separated Elongation Complex, PDB code: 1sfo:

Magnesium binding site 1 out of 1 in the Rna Polymerase II Strand Separated Elongation Complex


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 Strand Separated Elongation Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2000 b:22.8 occ:1.00 O3' R:A10 2.1 30.0 1.0 OD1 A:ASP481 2.1 1.0 1.0 OD2 A:ASP483 2.4 38.0 1.0 OD1 A:ASP485 2.6 30.0 1.0 OD1 A:ASP483 2.6 38.0 1.0 CG A:ASP483 2.8 38.0 1.0 CG A:ASP481 3.1 1.0 1.0 C3' R:A10 3.4 30.0 1.0 OD2 A:ASP481 3.5 1.0 1.0 CG A:ASP485 3.6 30.0 1.0 OD2 A:ASP485 3.9 30.0 1.0 C4' R:A10 4.0 30.0 1.0 C5' R:A10 4.0 30.0 1.0 CB A:ASP483 4.3 38.0 1.0 CB A:ASP481 4.4 1.0 1.0 C2' R:A10 4.5 30.0 1.0 O2' R:A10 4.7 30.0 1.0 N A:ASP481 4.8 34.9 1.0 N A:ASP483 4.8 30.0 1.0 CA A:ASP481 4.9 34.9 1.0 C A:ASP481 4.9 34.9 1.0

K.D.Westover, D.A.Bushnell, R.D.Kornberg. Structural Basis of Transcription: Separation of Rna From Dna By Rna Polymerase II Science V. 303 1014 2004.
ISSN: ISSN 0036-8075
PubMed: 14963331
DOI: 10.1126/SCIENCE.1090839