Magnesium in PDB 3ffa: Crystal Structure of A Fast Activating G Protein Mutant

The structure of Crystal Structure of A Fast Activating G Protein Mutant, PDB code: 3ffa was solved by R.Chauhan, N.Kapoor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.40 / 2.30
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.008, 79.008, 105.667, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 25.2

The binding sites of Magnesium atom in the Crystal Structure of A Fast Activating G Protein Mutant (pdb code 3ffa). 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 Crystal Structure of A Fast Activating G Protein Mutant, PDB code: 3ffa:

Magnesium binding site 1 out of 1 in the Crystal Structure of A Fast Activating G Protein Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Fast Activating G Protein Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg349 b:28.7 occ:1.00 OG1 A:THR181 2.5 24.9 1.0 O1B A:GSP1 2.6 8.2 1.0 O2G A:GSP1 2.9 33.9 1.0 OD1 A:ASP200 3.1 21.7 1.0 CB A:THR181 3.2 22.1 1.0 O A:VAL201 3.4 22.2 1.0 S1G A:GSP1 3.4 31.8 1.0 O A:HOH367 3.5 16.8 1.0 OD2 A:ASP200 3.5 19.8 1.0 PG A:GSP1 3.6 34.3 1.0 PB A:GSP1 3.7 9.2 1.0 CG A:ASP200 3.7 18.4 1.0 CB A:SER47 3.7 11.9 1.0 CE A:LYS46 3.9 11.1 1.0 O3B A:GSP1 3.9 16.6 1.0 CG2 A:THR181 4.0 22.0 1.0 N A:SER47 4.1 10.4 1.0 O2B A:GSP1 4.1 6.2 1.0 C A:VAL201 4.3 18.3 1.0 CB A:LYS46 4.3 8.1 1.0 NZ A:LYS46 4.3 11.2 1.0 CA A:SER47 4.4 11.6 1.0 CA A:THR181 4.4 23.5 1.0 CA A:GLY202 4.5 15.7 1.0 N A:THR181 4.6 22.1 1.0 OG A:SER47 4.7 20.8 1.0 N A:GLY202 4.7 16.7 1.0 CD A:LYS46 4.8 8.4 1.0 C A:LYS46 4.9 9.7 1.0

N.Kapoor, S.T.Menon, R.Chauhan, P.Sachdev, T.P.Sakmar. Structural Evidence For A Sequential Release Mechanism For Activation of Heterotrimeric G Proteins. J.Mol.Biol. V. 393 882 2009.
ISSN: ISSN 0022-2836
PubMed: 19703466
DOI: 10.1016/J.JMB.2009.08.043