Magnesium in PDB 3l86: The Crystal Structure of Smu.665 From Streptococcus Mutans UA159

All present enzymatic activity of The Crystal Structure of Smu.665 From Streptococcus Mutans UA159:
2.7.2.8;

The structure of The Crystal Structure of Smu.665 From Streptococcus Mutans UA159, PDB code: 3l86 was solved by X.-D.Su, X.Liu, C.W.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.93 / 2.06
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.190, 94.760, 47.580, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 26.7

The binding sites of Magnesium atom in the The Crystal Structure of Smu.665 From Streptococcus Mutans UA159 (pdb code 3l86). 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 The Crystal Structure of Smu.665 From Streptococcus Mutans UA159, PDB code: 3l86:

Magnesium binding site 1 out of 1 in the The Crystal Structure of Smu.665 From Streptococcus Mutans UA159


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of Smu.665 From Streptococcus Mutans UA159 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg248 b:10.7 occ:1.00 O2A A:ADP246 2.0 10.7 1.0 O A:HOH275 2.1 10.8 1.0 O1B A:ADP246 2.1 8.2 1.0 O A:HOH273 2.2 8.7 1.0 O A:HOH274 2.2 9.9 1.0 O A:HOH262 2.3 12.4 1.0 PA A:ADP246 3.2 11.7 1.0 PB A:ADP246 3.3 11.6 1.0 O3A A:ADP246 3.6 10.5 1.0 O3B A:ADP246 3.7 14.0 1.0 OD2 A:ASP160 4.0 14.9 1.0 O A:HOH286 4.0 15.5 1.0 NZ A:LYS215 4.1 5.0 1.0 O5' A:ADP246 4.1 11.0 1.0 O A:GLY211 4.4 11.8 1.0 OE1 A:NLG247 4.4 10.5 1.0 O1A A:ADP246 4.5 9.6 1.0 CA A:GLY211 4.5 12.0 1.0 OE2 A:NLG247 4.6 10.6 1.0 O2B A:ADP246 4.6 14.1 1.0 ND2 A:ASN158 4.6 14.3 1.0 CE A:LYS215 4.8 4.2 1.0 C A:GLY211 4.9 12.2 1.0 CD A:NLG247 4.9 12.4 1.0 CG A:ASP160 5.0 12.9 1.0

X.-D.Su, X.Liu, C.W.Wu. The Crystal Structure of Smu.665 From Streptococcus Mutans UA159 To Be Published.