Magnesium in PDB 6w2y: Cryoem Structure of GABAB1B Homodimer

The structure of Cryoem Structure of GABAB1B Homodimer also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Magnesium atom in the Cryoem Structure of GABAB1B Homodimer (pdb code 6w2y). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryoem Structure of GABAB1B Homodimer, PDB code: 6w2y:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryoem Structure of GABAB1B Homodimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of GABAB1B Homodimer within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg905 b:22.5 occ:1.00 O A:GLY277 2.2 30.6 1.0 OE1 A:GLU309 2.5 32.0 1.0 OE1 A:GLU423 2.9 36.7 1.0 C A:GLY277 3.2 30.6 1.0 CA A:GLY277 3.6 30.6 1.0 CD A:GLU309 3.7 32.0 1.0 O A:TYR279 3.8 37.0 1.0 CD A:GLU423 3.9 36.7 1.0 OD1 A:ASP281 4.0 47.7 1.0 OE2 A:GLU423 4.2 36.7 1.0 OE2 A:GLU309 4.3 32.0 1.0 N A:TRP278 4.4 35.5 1.0 CG2 A:THR307 4.8 34.6 1.0 CG A:GLU309 4.9 32.0 1.0 C A:TYR279 5.0 37.0 1.0

Magnesium binding site 2 out of 2 in the Cryoem Structure of GABAB1B Homodimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of GABAB1B Homodimer within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg905 b:21.8 occ:1.00 OE1 B:GLU309 2.4 31.6 1.0 O B:GLY277 2.4 28.9 1.0 OE1 B:GLU423 2.8 37.6 1.0 C B:GLY277 3.4 28.9 1.0 CD B:GLU309 3.5 31.6 1.0 CA B:GLY277 3.7 28.9 1.0 O B:TYR279 3.9 35.5 1.0 OE2 B:GLU309 4.0 31.6 1.0 CD B:GLU423 4.0 37.6 1.0 OE2 B:GLU423 4.5 37.6 1.0 N B:TRP278 4.6 32.5 1.0 CG B:GLU309 4.8 31.6 1.0

M.M.Papasergi-Scott, M.J.Robertson, A.B.Seven, O.Panova, J.M.Mathiesen, G.Skiniotis. Structures of Metabotropic Gababreceptor. Nature V. 584 310 2020.
ISSN: ESSN 1476-4687
PubMed: 32580208
DOI: 10.1038/S41586-020-2469-4