Magnesium in PDB 5vgt: X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7

The structure of X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7, PDB code: 5vgt was solved by L.Tang, L.Liang, H.Zhao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 1.78
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.297, 101.297, 76.465, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 23.4

The structure of X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7 also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Magnesium atom in the X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7 (pdb code 5vgt). 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 X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7, PDB code: 5vgt:

Magnesium binding site 1 out of 1 in the X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Structure of Bacteriophage SF6 Tail Adaptor Protein GP7 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg204 b:99.8 occ:1.00 O A:HOH302 2.4 24.2 1.0 O A:THR115 2.8 25.0 1.0 OD1 A:ASP116 3.4 35.8 1.0 O A:ALA112 3.7 24.1 1.0 CA A:ALA112 3.7 26.0 1.0 CA A:ASP116 3.7 23.6 1.0 C A:THR115 3.7 27.6 1.0 C A:ALA112 4.1 25.3 1.0 N A:ASP116 4.2 25.7 1.0 CG A:ASP116 4.3 35.1 1.0 CB A:ALA112 4.3 26.6 1.0 O A:HOH336 4.3 34.4 1.0 O A:ASP111 4.4 26.5 1.0 OG1 A:THR115 4.5 25.8 1.0 N A:THR117 4.5 23.6 1.0 C A:ASP116 4.5 24.9 1.0 CB A:ASP116 4.6 25.7 1.0 N A:ALA112 4.7 22.8 1.0 O A:HOH351 4.9 40.9 1.0 C A:ASP111 4.9 24.8 1.0 CA A:THR115 4.9 26.9 1.0

L.Liang, H.Zhao, B.An, L.Tang. High-Resolution Structure of Podovirus Tail Adaptor Suggests Repositioning of An Octad Motif That Mediates the Sequential Tail Assembly. Proc. Natl. Acad. Sci. V. 115 313 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29279385
DOI: 10.1073/PNAS.1706846115