Magnesium in PDB 6x50: Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State

All present enzymatic activity of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State:
2.7.7.6;

The structure of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State (pdb code 6x50). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State, PDB code: 6x50:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2001 b:19.8 occ:1.00 O3G A:ATP2000 2.1 28.3 1.0 OD1 A:ASP729 2.1 20.0 1.0 CG A:ASP729 2.8 20.0 1.0 OD2 A:ASP729 2.8 20.0 1.0 OG1 A:THR635 2.8 21.7 1.0 PG A:ATP2000 3.3 28.3 1.0 NE2 A:HIS665 3.4 15.1 1.0 O3B A:ATP2000 3.5 28.3 1.0 CE1 A:HIS665 3.6 15.1 1.0 O1G A:ATP2000 3.8 28.3 1.0 CD2 A:LEU754 4.0 19.0 1.0 CB A:THR635 4.0 21.7 1.0 OE2 A:GLU730 4.2 22.2 1.0 CB A:ASP729 4.2 20.0 1.0 CA A:THR635 4.4 21.7 1.0 CG2 A:THR635 4.4 21.7 1.0 O2G A:ATP2000 4.5 28.3 1.0 N A:THR635 4.6 21.7 1.0 CD2 A:HIS665 4.7 15.1 1.0 CB A:LEU754 4.8 19.0 1.0 O2A A:ATP2000 4.8 28.3 1.0 ND1 A:HIS665 4.9 15.1 1.0

Magnesium binding site 2 out of 2 in the Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mfd-Bound E.Coli Rna Polymerase Elongation Complex - V State within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg1501 b:23.7 occ:1.00 O3' R:A20 2.0 42.3 1.0 OD1 J:ASP460 2.0 22.3 1.0 OD1 J:ASP462 2.1 20.1 1.0 OD1 J:ASP464 2.2 27.0 1.0 CG J:ASP460 2.7 22.3 1.0 OD2 J:ASP460 2.8 22.3 1.0 CG J:ASP464 3.0 27.0 1.0 CG J:ASP462 3.1 20.1 1.0 OD2 J:ASP464 3.2 27.0 1.0 C3' R:A20 3.2 42.3 1.0 OD2 J:ASP462 3.5 20.1 1.0 O2' R:A20 3.5 42.3 1.0 C4' R:A20 3.7 42.3 1.0 C2' R:A20 3.9 42.3 1.0 CB J:ASP460 4.0 22.3 1.0 O J:ASP460 4.1 22.3 1.0 C5' R:A20 4.3 42.3 1.0 C J:ASP460 4.4 22.3 1.0 CB J:ASP464 4.4 27.0 1.0 N J:ASP460 4.5 22.3 1.0 N J:ASP462 4.5 20.1 1.0 CB J:ASP462 4.5 20.1 1.0 CA J:ASP460 4.5 22.3 1.0 NH2 J:ARG425 4.6 22.4 1.0 N J:ASP464 4.7 27.0 1.0 C J:ASP462 4.8 20.1 1.0 CA J:ASP462 4.8 20.1 1.0 CA J:ASP464 4.9 27.0 1.0 O4' R:A20 4.9 42.3 1.0 O J:ASP462 5.0 20.1 1.0

J.Y.Kang, E.Llewellyn, J.Chen, P.D.B.Olinares, J.Brewer, B.T.Chait, E.A.Campbell, S.A.Darst. Structural Basis For Transcription Complex Disruption By the Mfd Translocase. Elife V. 10 2021.
ISSN: ESSN 2050-084X
PubMed: 33480355
DOI: 10.7554/ELIFE.62117