Magnesium in PDB 2wzg: Legionella Glucosyltransferase (LGT1) Crystal Structure

The structure of Legionella Glucosyltransferase (LGT1) Crystal Structure, PDB code: 2wzg was solved by R.Hurtado-Guerrero, T.Zusman, S.Pathak, A.F.M.Ibrahim, S.Shepherd, A.Prescott, G.Segal, D.M.F.Van Aalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	122.750, 122.750, 103.416, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 26.2

The binding sites of Magnesium atom in the Legionella Glucosyltransferase (LGT1) Crystal Structure (pdb code 2wzg). 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 Legionella Glucosyltransferase (LGT1) Crystal Structure, PDB code: 2wzg:

Magnesium binding site 1 out of 1 in the Legionella Glucosyltransferase (LGT1) Crystal Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Legionella Glucosyltransferase (LGT1) Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1524 b:37.2 occ:1.00 O1A A:UPG1525 2.1 31.7 1.0 O A:HOH2318 2.1 46.3 1.0 O2B A:UPG1525 2.1 35.0 1.0 O A:HOH2166 2.2 36.7 1.0 PA A:UPG1525 3.3 33.8 1.0 OD2 A:ASP248 3.3 47.8 1.0 PB A:UPG1525 3.4 35.0 1.0 O3A A:UPG1525 3.7 33.6 1.0 OD1 A:ASP248 3.8 48.8 1.0 O A:HOH2313 3.9 32.9 1.0 O3B A:UPG1525 3.9 30.1 1.0 CG A:ASP248 4.0 43.8 1.0 OD2 A:ASP246 4.0 29.3 1.0 O2A A:UPG1525 4.0 32.4 1.0 OD1 A:ASN499 4.4 42.5 1.0 O A:HOH2001 4.5 46.2 1.0 O5C A:UPG1525 4.6 29.0 1.0 O2' A:UPG1525 4.6 34.8 1.0 O1B A:UPG1525 4.7 33.6 1.0 ND2 A:ASN499 4.8 41.2 1.0 C5C A:UPG1525 4.9 28.5 1.0 CG A:ASN499 4.9 40.4 1.0 CG A:ASP246 4.9 29.9 1.0

R.Hurtado-Guerrero, T.Zusman, S.Pathak, A.F.M.Ibrahim, S.Shepherd, A.Prescott, G.Segal, D.M.F.Van Aalten. Molecular Mechanism of Elongation Factor 1A Inhibition By A Legionella Pneumophila Glycosyltransferase. Biochem.J. V. 426 281 2010.
ISSN: ISSN 0264-6021
PubMed: 20030628
DOI: 10.1042/BJ20091351