Magnesium in PDB 8cnn: BEF3 Phospho-Hras Gsa Complex

All present enzymatic activity of BEF3 Phospho-Hras Gsa Complex:
3.6.5.2;

The structure of BEF3 Phospho-Hras Gsa Complex, PDB code: 8cnn was solved by P.Baumann, Y.Jin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.17 / 1.48
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	87.77, 87.77, 132.381, 90, 90, 120
R / Rfree (%)	16.4 / 18.8

The structure of BEF3 Phospho-Hras Gsa Complex also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

The binding sites of Magnesium atom in the BEF3 Phospho-Hras Gsa Complex (pdb code 8cnn). 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 BEF3 Phospho-Hras Gsa Complex, PDB code: 8cnn:

Magnesium binding site 1 out of 1 in the BEF3 Phospho-Hras Gsa Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of BEF3 Phospho-Hras Gsa Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg208 b:16.1 occ:1.00 F1 A:BEF207 2.0 17.3 1.0 O3B A:GDP206 2.0 15.4 1.0 OG A:SER17 2.0 16.5 1.0 O A:HOH315 2.1 16.0 1.0 O A:HOH336 2.1 15.9 1.0 OG1 A:THR35 2.1 16.6 1.0 CB A:THR35 3.1 16.4 1.0 CB A:SER17 3.2 15.9 1.0 BE A:BEF207 3.2 19.5 1.0 PB A:GDP206 3.2 16.6 1.0 O2B A:GDP206 3.4 16.3 1.0 N A:THR35 3.8 16.8 1.0 N A:SER17 3.9 14.8 1.0 OD2 A:ASP57 4.0 17.0 1.0 CA A:THR35 4.1 16.9 1.0 O A:HOH316 4.1 17.4 1.0 CA A:SER17 4.1 14.5 1.0 CG2 A:THR35 4.1 17.0 1.0 O2A A:GDP206 4.1 16.9 1.0 F2 A:BEF207 4.1 18.1 1.0 OD1 A:ASP57 4.2 17.0 1.0 O3A A:GDP206 4.2 15.4 1.0 O1B A:GDP206 4.3 15.1 1.0 F3 A:BEF207 4.3 18.6 1.0 O A:ASP33 4.4 17.8 1.0 PA A:GDP206 4.5 16.8 1.0 CG A:ASP57 4.5 17.6 1.0 O A:THR58 4.5 17.3 1.0 O1A A:GDP206 4.6 16.1 1.0 C A:PRO34 4.8 17.3 1.0 CB A:LYS16 4.8 16.4 1.0 CE A:LYS16 4.9 16.6 1.0 C A:LYS16 5.0 15.5 1.0

P.Baumann, Y.Jin. BEF3 Phospho-Hras Gsa Complex To Be Published.