Magnesium in PDB 6xre: Structure of the P53/Rna Polymerase II Assembly

Enzymatic activity of Structure of the P53/Rna Polymerase II Assembly

All present enzymatic activity of Structure of the P53/Rna Polymerase II Assembly:
2.7.7.6;

Other elements in 6xre:

The structure of Structure of the P53/Rna Polymerase II Assembly also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the P53/Rna Polymerase II Assembly (pdb code 6xre). 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 Structure of the P53/Rna Polymerase II Assembly, PDB code: 6xre:

Magnesium binding site 1 out of 1 in 6xre

Go back to Magnesium Binding Sites List in 6xre
Magnesium binding site 1 out of 1 in the Structure of the P53/Rna Polymerase II Assembly


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the P53/Rna Polymerase II Assembly within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:13.6
occ:1.00
OD2 A:ASP499 1.8 18.4 1.0
OD1 A:ASP497 1.9 19.2 1.0
OD1 A:ASP495 1.9 18.1 1.0
OD2 A:ASP495 2.1 18.1 1.0
CG A:ASP495 2.3 18.1 1.0
CG A:ASP497 2.4 19.2 1.0
OD2 A:ASP497 2.4 19.2 1.0
CG A:ASP499 2.6 18.4 1.0
OD1 A:ASP499 3.2 18.4 1.0
H A:ASP497 3.5 23.1 1.0
HB2 A:ASP499 3.6 22.0 1.0
CB A:ASP495 3.7 18.1 1.0
O A:ASP495 3.7 18.1 1.0
CB A:ASP499 3.7 18.4 1.0
CB A:ASP497 3.9 19.2 1.0
HB2 A:ASP495 4.0 21.7 1.0
H A:ASP495 4.2 21.7 1.0
C A:ASP495 4.2 18.1 1.0
HB3 A:ASP497 4.3 23.1 1.0
H A:ASP499 4.3 22.0 1.0
N A:ASP497 4.3 19.2 1.0
HB3 A:ASP499 4.4 22.0 1.0
HB3 A:ASP495 4.4 21.7 1.0
CA A:ASP495 4.5 18.1 1.0
CA A:ASP497 4.5 19.2 1.0
HB2 A:ASP497 4.6 23.1 1.0
N A:ASP499 4.7 18.4 1.0
C A:ASP497 4.7 19.2 1.0
N A:ASP495 4.8 18.1 1.0
CA A:ASP499 4.8 18.4 1.0

Reference:

S.-H.Liou, S.Singh, R.H.Singer, R.A.Coleman, W.Liu. Structure of the P53/Rna Polymerase II Assembly To Be Published 2021.
DOI: 10.1038/S42003-021-01934-4
Page generated: Sat Apr 3 16:42:01 2021

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