Magnesium in PDB 7nkx: Rna Polymerase II-SPT4/5-Nucleosome-CHD1 Structure

Enzymatic activity of Rna Polymerase II-SPT4/5-Nucleosome-CHD1 Structure

All present enzymatic activity of Rna Polymerase II-SPT4/5-Nucleosome-CHD1 Structure:
2.7.7.6;

Other elements in 7nkx:

The structure of Rna Polymerase II-SPT4/5-Nucleosome-CHD1 Structure also contains other interesting chemical elements:

Zinc (Zn) 8 atoms
Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rna Polymerase II-SPT4/5-Nucleosome-CHD1 Structure (pdb code 7nkx). 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-SPT4/5-Nucleosome-CHD1 Structure, PDB code: 7nkx:

Magnesium binding site 1 out of 1 in 7nkx

Go back to Magnesium Binding Sites List in 7nkx
Magnesium binding site 1 out of 1 in the Rna Polymerase II-SPT4/5-Nucleosome-CHD1 Structure


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-SPT4/5-Nucleosome-CHD1 Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1803

b:87.6
occ:1.00
O3' P:U46 2.0 80.0 1.0
OD1 A:ASP483 2.0 75.6 1.0
OD1 A:ASP485 2.1 77.1 1.0
CG A:ASP483 2.8 75.6 1.0
CG A:ASP485 2.9 77.1 1.0
OD2 A:ASP483 3.0 75.6 1.0
OD2 A:ASP485 3.2 77.1 1.0
C3' P:U46 3.3 80.0 1.0
CB A:ASP481 3.4 79.4 1.0
C4' P:U46 3.9 80.0 1.0
O2' P:U46 4.0 80.0 1.0
C2' P:U46 4.2 80.0 1.0
CB A:ASP483 4.2 75.6 1.0
CB A:ASP485 4.2 77.1 1.0
N A:ASP481 4.3 79.4 1.0
CA A:ASP481 4.3 79.4 1.0
NH2 A:ARG446 4.4 77.1 1.0
C5' P:U46 4.4 80.0 1.0
CG A:ASP481 4.5 79.4 1.0
OD2 A:ASP481 4.5 79.4 1.0
N A:ASP483 4.5 75.6 1.0
C A:ASP481 4.7 79.4 1.0
N A:ASP485 4.8 77.1 1.0
CA A:ASP485 4.8 77.1 1.0
CA A:ASP483 4.8 75.6 1.0
N A:PHE482 5.0 74.9 1.0

Reference:

L.Farnung, M.Ochmann, M.Engeholm, P.Cramer. Structural Basis of Nucleosome Transcription Mediated By CHD1 and Fact. Nat.Struct.Mol.Biol. V. 28 382 2021.
ISSN: ESSN 1545-9985
PubMed: 33846633
DOI: 10.1038/S41594-021-00578-6
Page generated: Fri Sep 24 15:26:21 2021

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