Magnesium in PDB 9exs: Cryo-Em Structure of Ch. Thermophilum RAI1-RAT1 Dimer.

The binding sites of Magnesium atom in the Cryo-Em Structure of Ch. Thermophilum RAI1-RAT1 Dimer. (pdb code 9exs). 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 Ch. Thermophilum RAI1-RAT1 Dimer., PDB code: 9exs:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of Ch. Thermophilum RAI1-RAT1 Dimer.


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 Ch. Thermophilum RAI1-RAT1 Dimer. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:50.0 occ:1.00 OD2 A:ASP217 1.9 98.1 1.0 OE2 A:GLU166 2.0 98.4 1.0 OE2 A:GLU235 2.0 98.6 1.0 O A:LEU236 2.1 98.8 1.0 H A:LEU236 2.7 98.8 1.0 CG A:ASP217 2.7 98.1 1.0 OD1 A:ASP217 2.8 98.1 1.0 CD A:GLU235 3.1 98.6 1.0 HB2 A:LEU236 3.1 98.8 1.0 CD A:GLU166 3.1 98.4 1.0 C A:LEU236 3.1 98.8 1.0 N A:LEU236 3.4 98.8 1.0 CA A:LEU236 3.6 98.8 1.0 OE1 A:GLU235 3.8 98.6 1.0 OE1 A:GLU166 3.8 98.4 1.0 HG3 A:GLU235 3.8 98.6 1.0 CB A:LEU236 3.9 98.8 1.0 HD3 A:LYS237 3.9 98.4 1.0 HG2 A:GLU166 4.0 98.4 1.0 CG A:GLU235 4.1 98.6 1.0 CB A:ASP217 4.1 98.1 1.0 CG A:GLU166 4.1 98.4 1.0 HA A:GLU235 4.2 98.6 1.0 N A:LYS237 4.3 98.4 1.0 HA A:LYS237 4.3 98.4 1.0 HB3 A:ASP217 4.4 98.1 1.0 HB2 A:ASP217 4.4 98.1 1.0 C A:GLU235 4.4 98.6 1.0 HB3 A:LEU236 4.5 98.8 1.0 HG2 A:LYS237 4.5 98.4 1.0 HG3 A:GLU166 4.6 98.4 1.0 HA A:LEU236 4.7 98.8 1.0 HE2 A:LYS237 4.7 98.4 1.0 CA A:GLU235 4.7 98.6 1.0 HG A:LEU236 4.8 98.8 1.0 CD A:LYS237 4.8 98.4 1.0 HG2 A:GLU235 4.8 98.6 1.0 CA A:LYS237 4.9 98.4 1.0 HZ1 A:LYS237 4.9 98.4 1.0 CG A:LEU236 5.0 98.8 1.0 CB A:GLU235 5.0 98.6 1.0

A.Dikunova, N.Noskova, J.H.Overbeck, M.Polak, D.Stelzig, D.Zapletal, K.Kubicek, J.Novacek, R.Sprangers, R.Stefl. Assembly of the XRN2/RAT1-RAI1-RTT103 Termination Complexes in Mesophilic and Thermophilic Organisms Structure 2024.
ISSN: ISSN 0969-2126
DOI: 10.1016/J.STR.2024.11.010