Magnesium in PDB 3mbo: Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate

The structure of Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate, PDB code: 3mbo was solved by B.D.Wallace, A.Claiborne, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.22 / 3.31
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	226.266, 226.266, 75.354, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 25.7

The binding sites of Magnesium atom in the Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate (pdb code 3mbo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate, PDB code: 3mbo:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg386 b:43.6 occ:1.00 O2A C:UDP382 2.7 65.7 1.0 OE2 C:GLU282 2.7 60.4 1.0 O1B C:UDP382 2.8 65.5 1.0 N C:GLY285 3.1 53.8 1.0 O C:HOH423 3.2 32.3 1.0 CA C:GLY285 3.6 54.8 1.0 PA C:UDP382 3.8 66.2 1.0 CD C:GLU282 3.9 58.7 1.0 N C:PHE284 4.0 50.1 1.0 PB C:UDP382 4.0 65.9 1.0 C C:PHE284 4.2 52.7 1.0 O3A C:UDP382 4.2 65.8 1.0 O1A C:UDP382 4.3 65.9 1.0 O4 C:MLT385 4.4 62.3 0.8 CA C:PHE284 4.4 51.3 1.0 NZ C:LYS211 4.4 55.3 1.0 N C:SER283 4.6 49.1 1.0 CG C:GLU282 4.6 54.8 1.0 CB C:PHE284 4.6 50.8 1.0 N C:LEU286 4.6 55.0 1.0 C C:GLY285 4.7 55.2 1.0 O2B C:UDP382 4.7 66.0 1.0 CA C:GLY121 4.8 46.3 1.0 O5 C:MLT385 4.9 62.8 0.8 OE1 C:GLU282 4.9 59.8 1.0 N C:GLY121 4.9 45.6 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Glycosyltransferase Babsha Bound with Udp and L-Malate within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg388 b:73.0 occ:1.00 O2A E:UDP382 2.7 85.4 1.0 OE2 E:GLU282 2.9 67.6 1.0 O E:HOH400 2.9 56.8 1.0 O E:PHE284 3.1 62.2 1.0 O3B E:UDP382 3.7 85.9 1.0 PA E:UDP382 3.9 85.4 0.8 CD E:GLU282 3.9 66.5 1.0 O1A E:UDP382 4.2 85.0 1.0 C E:PHE284 4.2 62.2 1.0 O3A E:UDP382 4.3 85.8 1.0 OE1 E:GLU282 4.3 67.3 1.0 O E:HOH420 4.5 79.3 1.0 N E:PHE284 4.6 62.5 1.0 PB E:UDP382 4.6 86.1 0.8 OG E:SER283 4.7 62.4 1.0 NZ E:LYS211 4.7 69.1 1.0 CA E:GLY285 4.8 62.0 1.0 CB E:SER283 4.8 62.5 1.0 N E:GLY285 4.9 62.2 1.0 N E:GLY121 4.9 49.5 1.0 N E:SER283 5.0 61.7 1.0

D.Parsonage, G.L.Newton, R.C.Holder, B.D.Wallace, C.Paige, P.C.Dos Santos, M.R.Redinbo, R.C.Fahey, S.D.Reid, A.Claiborne. Characterization of the N-Acetyl-Alpha-D-Glucosaminyl L-Malate Synthase and Deacetylase Functions For Bacillithiol Biosynthesis in Bacillus Anthracis Biochemistry V. 49 8398 2010.
ISSN: ISSN 0006-2960