Magnesium in PDB 8tvx: Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2)

All present enzymatic activity of Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2):
2.7.7.6;

The structure of Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2) also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Magnesium atom in the Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2) (pdb code 8tvx). 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 Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2), PDB code: 8tvx:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Cpd-Stalled Pol II (Conformation 2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1803 b:106.1 occ:1.00 OD2 A:ASP483 2.5 118.1 1.0 OD1 A:ASP483 2.6 118.1 1.0 OD1 A:ASP485 2.6 117.1 1.0 HB3 A:ASP481 2.7 120.4 1.0 OD2 A:ASP485 2.8 117.1 1.0 CG A:ASP483 2.8 118.1 1.0 CG A:ASP485 3.1 117.1 1.0 HO3' R:A10 3.1 132.4 1.0 CB A:ASP481 3.6 120.4 1.0 HH22 A:ARG446 3.7 117.1 1.0 HH21 A:ARG446 3.7 117.1 1.0 HB2 A:ASP481 3.8 120.4 1.0 O3' R:A10 3.9 132.4 1.0 OD2 A:ASP481 4.0 120.4 1.0 NH2 A:ARG446 4.0 117.1 1.0 CG A:ASP481 4.2 120.4 1.0 CB A:ASP483 4.3 118.1 1.0 H A:ASP483 4.3 118.1 1.0 HB3 A:ASP483 4.5 118.1 1.0 O A:ASP481 4.5 120.4 1.0 CB A:ASP485 4.6 117.1 1.0 CA A:ASP481 4.6 120.4 1.0 HB2 A:ASP483 4.8 118.1 1.0 C A:ASP481 4.8 120.4 1.0 H A:ASP485 4.9 117.1 1.0 N A:ASP481 4.9 120.4 1.0 H A:ASP481 4.9 120.4 1.0 H3' R:A10 4.9 132.4 1.0 HB2 A:ASP485 5.0 117.1 1.0

R.D.Sarsam, J.Xu, I.Lahiri, W.Gong, Q.Li, J.Oh, Z.Zhou, P.Hou, J.Chong, N.Hao, S.Li, D.Wang, A.E.Leschziner. ELF1 Promotes RAD26'S Interaction with Lesion-Arrested Pol II For Transcription-Coupled Repair. Proc.Natl.Acad.Sci.Usa V. 121 45121 2024.
ISSN: ESSN 1091-6490
PubMed: 38194460
DOI: 10.1073/PNAS.2314245121