Magnesium in PDB 3zi8: Structure of the R17A Mutant of the Ralstonia Soleanacerum Lectin at 1.5 Angstrom in Complex with L-Fucose

The structure of Structure of the R17A Mutant of the Ralstonia Soleanacerum Lectin at 1.5 Angstrom in Complex with L-Fucose, PDB code: 3zi8 was solved by J.Arnaud, A.Audfray, J.Claudinon, K.Trondle, M.Trosvalet, A.Thomas, A.Varrot, W.Romer, A.Imberty, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.20 / 1.50
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.399, 72.399, 35.990, 90.00, 90.00, 120.00
R / Rfree (%)	13.4 / 16.6

The binding sites of Magnesium atom in the Structure of the R17A Mutant of the Ralstonia Soleanacerum Lectin at 1.5 Angstrom in Complex with L-Fucose (pdb code 3zi8). 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 R17A Mutant of the Ralstonia Soleanacerum Lectin at 1.5 Angstrom in Complex with L-Fucose, PDB code: 3zi8:

Magnesium binding site 1 out of 1 in the Structure of the R17A Mutant of the Ralstonia Soleanacerum Lectin at 1.5 Angstrom in Complex with L-Fucose


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 R17A Mutant of the Ralstonia Soleanacerum Lectin at 1.5 Angstrom in Complex with L-Fucose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg101 b:20.5 occ:1.00 O A:HOH2020 2.3 17.0 1.0 O A:ALA7 2.3 12.6 1.0 O A:HOH2019 2.5 19.9 1.0 O A:HOH2018 2.7 10.8 0.5 C A:ALA7 3.4 11.7 1.0 N A:ALA7 4.1 11.5 1.0 CA A:ALA7 4.2 11.9 1.0 O A:HOH2021 4.3 17.2 1.0 N A:THR8 4.4 11.4 1.0 CB A:ALA7 4.5 13.4 1.0 O A:HOH2078 4.6 7.6 0.5 CA A:THR8 4.6 11.7 1.0 CG1 A:VAL50 4.9 12.6 1.0

J.Arnaud, J.Claudinon, K.Trondle, M.Trovaslet, G.Larson, A.Thomas, A.Varrot, W.Romer, A.Imberty, A.Audfray. Reduction of Lectin Valency Drastically Changes Glycolipid Dynamics in Membranes, But Not Surface Avidity. Acs Chem.Biol. V. 8 1918 2013.
ISSN: ISSN 1554-8929
PubMed: 23855446
DOI: 10.1021/CB400254B