Manganese in PDB 1i50: Rna Polymerase II Crystal Form II at 2.8 A Resolution

All present enzymatic activity of Rna Polymerase II Crystal Form II at 2.8 A Resolution:
2.7.7.6;

The structure of Rna Polymerase II Crystal Form II at 2.8 A Resolution, PDB code: 1i50 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 / 2.80
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	122.700, 223.000, 376.100, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 28.2

The structure of Rna Polymerase II Crystal Form II at 2.8 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Manganese atom in the Rna Polymerase II Crystal Form II at 2.8 A Resolution (pdb code 1i50). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Rna Polymerase II Crystal Form II at 2.8 A Resolution, PDB code: 1i50:

Manganese binding site 1 out of 1 in the Rna Polymerase II Crystal Form II at 2.8 A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Rna Polymerase II Crystal Form II at 2.8 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn3009 b:40.7 occ:1.00 OD1 A:ASP481 2.0 33.0 1.0 OD2 A:ASP483 2.2 36.8 1.0 OD2 A:ASP485 2.3 38.3 1.0 CG A:ASP481 2.7 34.5 1.0 OD2 A:ASP481 2.7 38.6 1.0 CG A:ASP483 3.0 40.7 1.0 OD1 A:ASP483 3.2 41.8 1.0 CG A:ASP485 3.2 34.4 1.0 OD1 A:ASP485 3.4 28.8 1.0 CB A:ASP481 4.2 28.1 1.0 CB A:ASP483 4.5 40.5 1.0 N A:ASP483 4.6 39.6 1.0 CB A:ASP485 4.6 33.2 1.0 N A:ASP485 4.6 34.1 1.0 N A:ASP481 4.7 31.5 1.0 C A:ASP481 4.8 33.4 1.0 CA A:ASP481 4.8 31.9 1.0 O A:ASP481 4.8 32.5 1.0 C A:ASP483 4.9 38.7 1.0 CA A:ASP483 4.9 39.3 1.0 CA A:ASP485 5.0 33.4 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