Magnesium in PDB 8p27: Cryo-Em Structure of the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State

The binding sites of Magnesium atom in the Cryo-Em Structure of the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State (pdb code 8p27). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State, PDB code: 8p27:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State


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 the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:47.2 occ:1.00 O2B B:DTP801 2.0 47.4 1.0 O3B B:DTP801 2.0 47.4 1.0 O2A B:DTP801 2.3 47.4 1.0 PB B:DTP801 2.4 47.4 1.0 O3G B:DTP801 2.5 47.4 1.0 OE1 A:GLU293 2.7 46.6 1.0 PG B:DTP801 2.8 47.4 1.0 O3A B:DTP801 3.0 47.4 1.0 OE1 A:GLN290 3.2 46.3 1.0 PA B:DTP801 3.3 47.4 1.0 NE2 A:GLN290 3.6 46.3 1.0 CD A:GLU293 3.6 46.6 1.0 O2G B:DTP801 3.7 47.4 1.0 O1B B:DTP801 3.8 47.4 1.0 OE2 A:GLU293 3.8 46.6 1.0 CD A:GLN290 3.8 46.3 1.0 O1G B:DTP801 4.0 47.4 1.0 O5' B:DTP801 4.2 47.4 1.0 NH2 B:ARG196 4.3 47.5 1.0 O1A B:DTP801 4.4 47.4 1.0 NH2 B:ARG192 4.6 49.0 1.0 C5' B:DTP801 5.0 47.4 1.0 NH1 B:ARG196 5.0 47.5 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of the Anaerobic Ribonucleotide Reductase From Prevotella Copri in Its Dimeric, Datp-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg802 b:47.3 occ:1.00 O3B A:DTP801 1.9 47.1 1.0 O2B A:DTP801 2.1 47.1 1.0 O2A A:DTP801 2.2 47.1 1.0 PB A:DTP801 2.4 47.1 1.0 O3G A:DTP801 2.7 47.1 1.0 OE1 B:GLU293 2.8 46.6 1.0 PG A:DTP801 2.9 47.1 1.0 O3A A:DTP801 2.9 47.1 1.0 OE1 B:GLN290 3.1 46.4 1.0 PA A:DTP801 3.1 47.1 1.0 CD B:GLU293 3.7 46.6 1.0 O1B A:DTP801 3.8 47.1 1.0 O1G A:DTP801 3.8 47.1 1.0 NE2 B:GLN290 3.8 46.4 1.0 CD B:GLN290 3.9 46.4 1.0 OE2 B:GLU293 3.9 46.6 1.0 O5' A:DTP801 4.0 47.1 1.0 O2G A:DTP801 4.0 47.1 1.0 NH2 A:ARG196 4.0 49.0 1.0 O1A A:DTP801 4.3 47.1 1.0 NH2 A:ARG192 4.6 48.2 1.0 C3' A:DTP801 5.0 47.1 1.0 C5' A:DTP801 5.0 47.1 1.0

O.Bimai, I.Banerjee, I.Rozman Grinberg, P.Huang, D.Lundin, B.M.Sjoberg, D.T.Logan. Activity Modulation in Anaerobic Ribonucleotide Reductases: Nucleotide Binding to the Atp-Cone Mediates Long-Range Order-Disorder Transitions in the Active Site Elife 2023.
ISSN: ESSN 2050-084X
DOI: 10.7554/ELIFE.89292.1