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Magnesium in PDB 3fki: 12-Subunit Rna Polymerase II Refined with Zn-Sad Data

Enzymatic activity of 12-Subunit Rna Polymerase II Refined with Zn-Sad Data

All present enzymatic activity of 12-Subunit Rna Polymerase II Refined with Zn-Sad Data:
2.7.7.6;

Protein crystallography data

The structure of 12-Subunit Rna Polymerase II Refined with Zn-Sad Data, PDB code: 3fki was solved by P.A.Meyer, P.Ye, M.H.Suh, M.Zhang, J.Fu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.22 / 3.88
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 220.581, 391.537, 280.734, 90.00, 90.00, 90.00
R / Rfree (%) 28.2 / 30.1

Other elements in 3fki:

The structure of 12-Subunit Rna Polymerase II Refined with Zn-Sad Data also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 12-Subunit Rna Polymerase II Refined with Zn-Sad Data (pdb code 3fki). 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 12-Subunit Rna Polymerase II Refined with Zn-Sad Data, PDB code: 3fki:

Magnesium binding site 1 out of 1 in 3fki

Go back to Magnesium Binding Sites List in 3fki
Magnesium binding site 1 out of 1 in the 12-Subunit Rna Polymerase II Refined with Zn-Sad Data


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 12-Subunit Rna Polymerase II Refined with Zn-Sad Data within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1736

b:0.0
occ:1.00
OD1 A:ASP483 2.5 81.2 1.0
OD2 A:ASP481 2.6 80.9 1.0
CG A:ASP481 3.5 80.8 1.0
CG A:ASP483 3.5 81.4 1.0
OD1 A:ASP481 3.6 80.5 1.0
OD2 A:ASP483 3.8 81.6 1.0
OD1 A:ASP485 3.8 80.0 1.0
CG A:ASP485 4.7 79.8 1.0
CB A:ASP481 4.8 80.9 1.0
O A:ASP483 4.8 80.8 1.0
OD2 A:ASP485 4.9 79.9 1.0
CB A:ASP483 4.9 81.4 1.0

Reference:

P.A.Meyer, P.Ye, M.H.Suh, M.Zhang, J.Fu. Structure of the 12-Subunit Rna Polymerase II Refined with the Aid of Anomalous Diffraction Data J.Biol.Chem. V. 284 12933 2009.
ISSN: ISSN 0021-9258
PubMed: 19289466
DOI: 10.1074/JBC.M809199200
Page generated: Wed Aug 14 13:49:19 2024

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