Magnesium in PDB 3ext: Crystal Structure of Kgpdc From Streptococcus Mutans

All present enzymatic activity of Crystal Structure of Kgpdc From Streptococcus Mutans:
4.1.1.85;

The structure of Crystal Structure of Kgpdc From Streptococcus Mutans, PDB code: 3ext was solved by X.Liu, G.L.Li, L.F.Li, X.D.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.75 / 2.00
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	83.780, 83.780, 171.620, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 22.2

The binding sites of Magnesium atom in the Crystal Structure of Kgpdc From Streptococcus Mutans (pdb code 3ext). 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 Crystal Structure of Kgpdc From Streptococcus Mutans, PDB code: 3ext:

Magnesium binding site 1 out of 1 in the Crystal Structure of Kgpdc From Streptococcus Mutans


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 Kgpdc From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg222 b:31.0 occ:1.00 O A:HOH303 1.9 28.6 1.0 OD2 A:ASP64 1.9 22.9 1.0 OE2 A:GLU35 2.1 22.2 1.0 O A:HOH304 2.1 26.7 1.0 O A:HOH301 2.3 36.5 1.0 O A:HOH302 2.3 33.5 1.0 CG A:ASP64 2.9 21.1 1.0 CD A:GLU35 3.1 23.9 1.0 OE1 A:GLU35 3.5 23.0 1.0 CB A:ASP64 3.7 19.0 1.0 OE2 A:GLU117 3.7 29.9 1.0 OD1 A:ASP64 3.8 25.6 1.0 NZ A:LYS66 3.8 24.8 1.0 O A:HOH293 4.1 36.8 1.0 O A:HOH256 4.3 41.3 1.0 CG A:GLU35 4.4 20.3 1.0 OD1 A:ASP13 4.5 29.1 1.0 O A:HOH224 4.6 21.6 1.0 CA A:GLY37 4.6 17.0 1.0 OG1 A:THR38 4.9 20.0 1.0 CD A:GLU117 4.9 26.4 1.0 O A:HOH268 5.0 29.2 1.0 N A:THR38 5.0 17.3 1.0

G.L.Li, X.Liu, J.Nan, E.Brostromer, L.F.Li, X.D.Su. Open-Closed Conformational Change Revealed By the Crystal Structures of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase From Streptococcus Mutans Biochem.Biophys.Res.Commun. V. 381 429 2009.
ISSN: ISSN 0006-291X
PubMed: 19222992
DOI: 10.1016/J.BBRC.2009.02.049