Magnesium in PDB 6a5t: Rna Polymerase II Elongation Complex Stalled at Shl(-1) of the Nucleosome

Enzymatic activity of Rna Polymerase II Elongation Complex Stalled at Shl(-1) of the Nucleosome

All present enzymatic activity of Rna Polymerase II Elongation Complex Stalled at Shl(-1) of the Nucleosome:
2.7.7.6;

Other elements in 6a5t:

The structure of Rna Polymerase II Elongation Complex Stalled at Shl(-1) of the Nucleosome also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rna Polymerase II Elongation Complex Stalled at Shl(-1) of the Nucleosome (pdb code 6a5t). 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 Elongation Complex Stalled at Shl(-1) of the Nucleosome, PDB code: 6a5t:

Magnesium binding site 1 out of 1 in 6a5t

Go back to Magnesium Binding Sites List in 6a5t
Magnesium binding site 1 out of 1 in the Rna Polymerase II Elongation Complex Stalled at Shl(-1) of the Nucleosome


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 Elongation Complex Stalled at Shl(-1) of the Nucleosome within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1803

b:47.7
occ:1.00
O3' P:G10 1.8 70.9 1.0
OD2 A:ASP484 2.3 54.0 1.0
OD1 A:ASP484 2.3 54.0 1.0
CG A:ASP484 2.6 54.0 1.0
OD1 A:ASP482 2.9 54.6 1.0
OD2 A:ASP482 3.0 54.6 1.0
C3' P:G10 3.1 70.9 1.0
OD1 A:ASP486 3.3 54.7 1.0
CG A:ASP482 3.4 54.6 1.0
C2' P:G10 4.0 70.9 1.0
CG A:ASP486 4.1 54.7 1.0
CB A:ASP484 4.1 54.0 1.0
C4' P:G10 4.2 70.9 1.0
O2' P:G10 4.2 70.9 1.0
OD2 A:ASP486 4.3 54.7 1.0
C5' P:G10 4.6 70.9 1.0
O5' P:G10 4.7 70.9 1.0
CB A:ASP482 4.9 54.6 1.0
NH2 A:ARG447 4.9 51.0 1.0
CA A:ASP484 5.0 54.0 1.0

Reference:

T.Kujirai, H.Ehara, Y.Fujino, M.Shirouzu, S.I.Sekine, H.Kurumizaka. Structural Basis of the Nucleosome Transition During Rna Polymerase II Passage. Science V. 362 595 2018.
ISSN: ESSN 1095-9203
PubMed: 30287617
DOI: 10.1126/SCIENCE.AAU9904
Page generated: Mon Dec 14 22:19:35 2020

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