Magnesium in PDB 5ll6: Structure of the 40S ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation

The structure of Structure of the 40S ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation also contains other interesting chemical elements:

Iron

(Fe)

8 atoms

The binding sites of Magnesium atom in the Structure of the 40S ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation (pdb code 5ll6). 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 Structure of the 40S ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation, PDB code: 5ll6:

Magnesium binding site 1 out of 1 in the Structure of the 40S ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the 40S ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation within 5.0Å range: probe atom residue distance (Å) B Occ h:Mg704 b:79.8 occ:1.00 OG h:SER117 2.2 60.7 1.0 O2B h:ANP703 2.2 59.5 1.0 O3G h:ANP703 2.2 52.4 1.0 OE1 h:GLN171 2.2 0.2 1.0 OG h:SER469 2.2 0.1 1.0 N3B h:ANP703 2.9 46.0 1.0 PB h:ANP703 2.9 50.0 1.0 PG h:ANP703 3.0 45.1 1.0 CD h:GLN171 3.1 0.9 1.0 CB h:SER117 3.3 59.2 1.0 O2A h:ANP703 3.3 42.2 1.0 O3A h:ANP703 3.4 46.9 1.0 O2G h:ANP703 3.6 46.7 1.0 CB h:SER469 3.6 0.8 1.0 NE2 h:GLN171 3.8 0.7 1.0 PA h:ANP703 3.9 40.1 1.0 N h:GLY470 3.9 0.2 1.0 CG h:GLN171 4.1 0.7 1.0 O1G h:ANP703 4.3 51.0 1.0 O1B h:ANP703 4.4 50.7 1.0 O1A h:ANP703 4.4 36.1 1.0 CA h:SER469 4.5 0.5 1.0 CA h:SER117 4.5 59.6 1.0 N h:SER117 4.5 49.1 1.0 C h:SER469 4.7 0.0 1.0 CA h:GLY470 4.8 0.0 1.0 OD2 h:ASP246 4.9 0.9 1.0

A.Heuer, M.Gerovac, C.Schmidt, S.Trowitzsch, A.Preis, P.Kotter, O.Berninghausen, T.Becker, R.Beckmann, R.Tampe. Structure of the 40S-ABCE1 Post-Splitting Complex in Ribosome Recycling and Translation Initiation. Nat. Struct. Mol. Biol. V. 24 453 2017.
ISSN: ESSN 1545-9985
PubMed: 28368393
DOI: 10.1038/NSMB.3396