Magnesium in PDB 5e9t: Crystal Structure of Gtfa/B Complex

The structure of Crystal Structure of Gtfa/B Complex, PDB code: 5e9t was solved by Y.Chen, T.A.Rapoport, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	122.12 / 2.92
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	155.930, 196.410, 220.860, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 27.5

The binding sites of Magnesium atom in the Crystal Structure of Gtfa/B Complex (pdb code 5e9t). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Gtfa/B Complex, PDB code: 5e9t:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Gtfa/B Complex


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 Gtfa/B Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:14.3 occ:1.00 OE1 A:GLU230 3.5 35.0 1.0 OD1 D:ASP83 3.9 37.2 1.0 OD2 D:ASP83 4.0 38.1 1.0 NE1 D:TRP70 4.4 14.1 1.0 CG D:ASP83 4.4 32.5 1.0 CD A:GLU230 4.5 30.8 1.0 NE2 A:GLN226 4.7 18.9 1.0 OE2 A:GLU230 4.8 24.2 1.0 NH2 A:ARG202 4.9 48.9 1.0 NH1 A:ARG202 4.9 49.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Gtfa/B Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Gtfa/B Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:20.9 occ:1.00 OD1 B:ASP83 3.8 44.3 1.0 OD2 B:ASP83 3.8 40.9 1.0 OE1 C:GLU230 4.0 53.1 1.0 CG B:ASP83 4.3 40.7 1.0 NE1 B:TRP70 4.5 17.8 1.0 OE2 C:GLU230 4.5 48.8 1.0 NH2 C:ARG202 4.6 40.6 1.0 CD C:GLU230 4.7 48.5 1.0

Y.Chen, R.Seepersaud, B.A.Bensing, P.M.Sullam, T.A.Rapoport. Mechanism of A Cytosolic O-Glycosyltransferase Essential For the Synthesis of A Bacterial Adhesion Protein. Proc.Natl.Acad.Sci.Usa V. 113 E1190 2016.
ISSN: ESSN 1091-6490
PubMed: 26884191
DOI: 10.1073/PNAS.1600494113