Magnesium in PDB 4zm1: Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type

The structure of Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type, PDB code: 4zm1 was solved by D.J.Ericsson, C.-W.Chang, T.Lonhienne, L.Casey, F.Benning, B.Kobe, E.N.H.Tran, R.Morona, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.68 / 2.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.890, 61.310, 90.860, 90.00, 94.21, 90.00
R / Rfree (%)	19.3 / 22.5

The binding sites of Magnesium atom in the Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type (pdb code 4zm1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type, PDB code: 4zm1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg301 b:48.7 occ:1.00 OG1 C:THR163 3.1 72.7 1.0 CB C:LYS164 4.0 65.2 1.0 N C:LYS164 4.1 58.9 1.0 CG C:LYS164 4.2 82.9 1.0 CB C:THR163 4.5 65.8 1.0 CD C:LYS164 4.5 98.7 1.0 N C:THR163 4.6 55.2 1.0 NE2 C:GLN166 4.7 93.0 1.0 CA C:LYS164 4.7 58.5 1.0 CA C:THR163 5.0 56.4 1.0 C C:THR163 5.0 61.9 1.0

Magnesium binding site 2 out of 2 in the Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Shigella Flexneri Lipopolysaccharide O-Antigen Chain-Length Regulator Wzzbsf - Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg302 b:51.0 occ:1.00 O C:PRO197 2.5 38.2 1.0 O C:HOH415 2.6 56.0 1.0 O C:HOH407 3.1 41.4 1.0 C C:PRO197 3.4 38.0 1.0 CD C:LYS143 3.6 38.9 1.0 CB C:LYS143 3.6 39.5 1.0 CA C:LEU198 3.7 35.1 1.0 CG C:LYS143 3.7 36.4 1.0 O C:HOH404 3.8 29.4 1.0 N C:LEU198 3.9 35.2 1.0 N C:VAL199 4.0 41.9 1.0 NE C:ARG196 4.1 44.5 1.0 CD C:ARG196 4.1 42.7 1.0 CG C:ARG196 4.1 36.6 1.0 C C:LEU198 4.2 44.4 1.0 O C:ARG196 4.3 37.3 1.0 CG1 C:VAL199 4.3 46.3 1.0 CA C:LYS143 4.3 38.7 1.0 CD2 C:LEU198 4.4 32.2 1.0 C C:ARG196 4.6 36.2 1.0 CG2 C:VAL199 4.6 49.3 1.0 CA C:PRO197 4.7 31.7 1.0 N C:PRO197 4.7 31.8 1.0 CE C:LYS143 4.8 30.9 1.0 CB C:LEU198 4.9 34.3 1.0 CB C:VAL199 4.9 48.5 1.0 CB C:ARG196 5.0 32.4 1.0

C.W.Chang, E.N.Tran, D.J.Ericsson, L.W.Casey, T.Lonhienne, F.Benning, R.Morona, B.Kobe. Structural and Biochemical Analysis of A Single Amino-Acid Mutant of Wzzbsf That Alters Lipopolysaccharide O-Antigen Chain Length in Shigella Flexneri. Plos One V. 10 38266 2015.
ISSN: ESSN 1932-6203
PubMed: 26378781
DOI: 10.1371/JOURNAL.PONE.0138266