Magnesium in PDB 8agg: Structure of the Legionella Phosphocholine Hydrolase LEM3

The structure of Structure of the Legionella Phosphocholine Hydrolase LEM3, PDB code: 8agg was solved by M.S.Kaspers, A.Itzen, V.Pogenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.54 / 3.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.022, 78.022, 382.014, 90, 90, 120
R / Rfree (%)	26.3 / 29.9

The binding sites of Magnesium atom in the Structure of the Legionella Phosphocholine Hydrolase LEM3 (pdb code 8agg). 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 Structure of the Legionella Phosphocholine Hydrolase LEM3, PDB code: 8agg:

Magnesium binding site 1 out of 1 in the Structure of the Legionella Phosphocholine Hydrolase LEM3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Legionella Phosphocholine Hydrolase LEM3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:196.3 occ:1.00 OD2 A:ASP105 2.1 191.4 1.0 OD2 A:ASP254 2.1 157.9 1.0 OD1 A:ASP254 2.1 178.5 1.0 OD1 A:ASP394 2.2 180.1 1.0 OD2 A:ASP394 2.2 190.9 1.0 OD1 A:ASP105 2.2 147.2 1.0 CG A:ASP394 2.4 169.5 1.0 CG A:ASP254 2.4 140.2 1.0 CG A:ASP105 2.5 159.6 1.0 CB A:ASP394 3.8 167.3 1.0 O A:CYS395 3.9 162.5 1.0 CB A:ASP254 3.9 150.6 1.0 CB A:ASP105 4.0 140.4 1.0 OD1 A:ASP82 4.3 158.2 1.0 N A:CYS395 4.3 162.5 1.0 OD2 A:ASP82 4.4 135.6 1.0 N A:ASP254 4.6 160.2 1.0 N A:GLY255 4.7 152.3 1.0 CA A:ASP254 4.8 152.9 1.0 CG A:ASP82 4.8 154.7 1.0 C A:CYS395 4.8 153.6 1.0 CA A:ASP394 4.8 158.1 1.0 CB A:CYS395 4.8 157.6 1.0 O A:GLY106 4.8 128.1 1.0 CA A:CYS395 4.9 147.3 1.0 CA A:ASP105 4.9 122.0 1.0 C A:ASP394 4.9 160.9 1.0

M.S.Kaspers, V.Pogenberg, S.Ernst, F.Ecker, C.Hedberg, M.Groll, A.Itzen. Dephosphocholination By Legionella Effector LEM3 Functions Through Remodelling of the Switch II Region of RAB1B Nat Commun 2023.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-023-37621-7