Magnesium in PDB 8hsg: Thermus Thermophilus Rna Polymerase Elongation Complex

All present enzymatic activity of Thermus Thermophilus Rna Polymerase Elongation Complex:
2.7.7.6;

The structure of Thermus Thermophilus Rna Polymerase Elongation Complex also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Thermus Thermophilus Rna Polymerase Elongation Complex (pdb code 8hsg). 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 Thermus Thermophilus Rna Polymerase Elongation Complex, PDB code: 8hsg:

Magnesium binding site 1 out of 1 in the Thermus Thermophilus Rna Polymerase Elongation Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Thermus Thermophilus Rna Polymerase Elongation Complex within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg1602 b:90.3 occ:1.00 OD1 J:ASP739 2.1 83.0 1.0 O3' R:C28 2.1 90.6 1.0 OP1 R:U29 2.1 95.0 1.0 OD1 J:ASP741 2.1 82.9 1.0 P R:U29 2.5 95.0 1.0 CG J:ASP741 3.0 82.9 1.0 CG J:ASP739 3.0 83.0 1.0 OD2 J:ASP741 3.1 82.9 1.0 OD2 J:ASP743 3.1 86.6 1.0 OD2 J:ASP739 3.3 83.0 1.0 CG J:ASP743 3.3 86.6 1.0 C3' R:C28 3.4 90.6 1.0 OP2 R:U29 3.5 95.0 1.0 CB J:ASP743 3.5 86.6 1.0 O2' R:C28 3.7 90.6 1.0 O5' R:U29 3.8 95.0 1.0 C4' R:C28 4.0 90.6 1.0 OD1 J:ASP743 4.0 86.6 1.0 C2' R:C28 4.1 90.6 1.0 N J:ASP739 4.3 83.0 1.0 CB J:ASP739 4.3 83.0 1.0 N J:ASP743 4.4 86.6 1.0 CB J:ASP741 4.4 82.9 1.0 N J:ASP741 4.5 82.9 1.0 CA J:ASP743 4.5 86.6 1.0 C5' R:U29 4.6 95.0 1.0 NH2 J:ARG704 4.6 76.6 1.0 C J:ASP739 4.6 83.0 1.0 C5' R:C28 4.7 90.6 1.0 CA J:ASP739 4.7 83.0 1.0 O J:ASP739 4.7 83.0 1.0 CA J:ASP741 4.9 82.9 1.0 C J:ASP741 5.0 82.9 1.0

Y.Murayama, H.Ehara, M.Aoki, M.Goto, T.Yokoyama, S.I.Sekine. Structural Basis of the Transcription Termination Factor Rho Engagement with Transcribing Rna Polymerase From Thermus Thermophilus. Sci Adv V. 9 E7093 2023.
ISSN: ESSN 2375-2548
PubMed: 36753546
DOI: 10.1126/SCIADV.ADE7093