Magnesium in PDB 4gwi: His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y

The structure of His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y, PDB code: 4gwi was solved by S.C.Feil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.95 / 1.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.097, 67.097, 99.432, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 19

The structure of His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y (pdb code 4gwi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y, PDB code: 4gwi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:20.0 occ:0.80 O A:HOH1215 2.0 27.0 1.0 O A:HOH1125 2.0 23.5 1.0 O A:HOH1214 2.1 24.5 1.0 O A:HOH1211 2.1 26.3 1.0 O A:HOH1213 2.1 25.6 1.0 NE2 A:HIS80 2.2 19.9 1.0 CE1 A:HIS80 3.2 20.1 1.0 CD2 A:HIS80 3.2 21.6 1.0 OD1 A:ASP77 4.3 23.5 1.0 O A:HOH1206 4.3 45.2 1.0 ND1 A:HIS80 4.3 19.6 1.0 CG A:HIS80 4.3 19.9 1.0 O A:HOH1160 4.9 31.6 1.0 CG A:ASP77 5.0 25.0 1.0

Magnesium binding site 2 out of 2 in the His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of His 62 Mutant of the Lectin Binding Domain of Lectinolysin Complexed with Lewis Y within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg203 b:38.8 occ:1.00 O A:HOH1193 1.9 36.5 1.0 O A:HOH1175 2.2 36.3 1.0 OD2 A:ASP97 2.2 22.7 1.0 O A:HOH1177 2.2 33.8 1.0 OE1 A:GLN54 2.4 48.8 1.0 CG A:ASP97 3.3 19.7 1.0 O A:HOH1161 3.6 34.2 1.0 CD A:GLN54 3.6 39.9 1.0 CB A:ASP97 3.7 18.5 1.0 NH2 A:ARG160 4.1 28.8 1.0 NE2 A:GLN54 4.2 39.5 1.0 OH A:TYR161 4.2 24.4 1.0 OD1 A:ASP97 4.4 22.0 1.0 CE2 A:TYR161 4.4 21.1 1.0 CG A:GLN54 4.7 29.5 1.0 O A:HOH1129 4.8 40.0 1.0 CZ A:TYR161 4.8 23.1 1.0 CB A:GLN54 4.9 21.2 1.0

S.L.Lawrence, S.C.Feil, J.K.Holien, M.J.Kuiper, L.Doughty, O.Dolezal, T.D.Mulhern, R.K.Tweten, M.W.Parker. Manipulating the Lewis Antigen Specificity of the Cholesterol-Dependent Cytolysin Lectinolysin Front Immunol V. 3 330 2012.
ISSN: ESSN 1664-3224
PubMed: 23181061
DOI: 10.3389/FIMMU.2012.00330