Magnesium in PDB 3e4g: Crystal Structure of Bovine Coupling Factor B, G28E Mutant

All present enzymatic activity of Crystal Structure of Bovine Coupling Factor B, G28E Mutant:
3.6.3.14;

The structure of Crystal Structure of Bovine Coupling Factor B, G28E Mutant, PDB code: 3e4g was solved by R.M.Stroud, J.K.Lee, G.I.Belogrudov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 0.96
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	107.476, 50.010, 36.886, 90.00, 109.37, 90.00
R / Rfree (%)	14.3 / 16.4

The binding sites of Magnesium atom in the Crystal Structure of Bovine Coupling Factor B, G28E Mutant (pdb code 3e4g). 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 Bovine Coupling Factor B, G28E Mutant, PDB code: 3e4g:

Magnesium binding site 1 out of 1 in the Crystal Structure of Bovine Coupling Factor B, G28E 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 Bovine Coupling Factor B, G28E Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg176 b:11.2 occ:1.00 O A:GLY34 2.2 11.0 1.0 O A:THR68 2.3 8.8 1.0 O A:HOH208 2.4 12.7 1.0 O A:HOH228 2.4 15.9 1.0 O A:HOH229 2.5 12.7 1.0 O A:HOH197 2.6 8.5 1.0 C A:GLY34 3.4 8.4 1.0 C A:THR68 3.5 7.7 1.0 O A:HOH392 3.9 25.0 1.0 N A:THR68 4.0 7.4 1.0 O A:HOH210 4.1 12.3 1.0 CA A:THR68 4.1 7.8 1.0 O A:ASP69 4.3 10.8 1.0 CA A:GLY34 4.3 8.2 1.0 CB A:THR68 4.3 9.0 1.0 N A:ALA35 4.3 7.3 1.0 O A:HOH406 4.3 33.3 1.0 CA A:ALA35 4.4 7.0 1.0 C A:ASP69 4.5 8.8 1.0 O A:HOH393 4.5 28.3 1.0 N A:ASP69 4.6 7.9 1.0 O A:HOH209 4.6 14.3 1.0 CB A:ASP69 4.6 9.7 1.0 O A:HOH227 4.7 11.3 1.0 CE A:MET36 4.7 14.0 1.0 CA A:ASP69 4.8 8.4 1.0 C A:ALA35 4.9 7.3 1.0 CG2 A:THR68 5.0 10.3 1.0

J.K.Lee, G.I.Belogrudov, R.M.Stroud. Crystal Structure of Bovine Mitochondrial Factor B at 0.96-A Resolution. Proc.Natl.Acad.Sci.Usa V. 105 13379 2008.
ISSN: ISSN 0027-8424
PubMed: 18768789
DOI: 10.1073/PNAS.0805689105