Magnesium in PDB 4az7: Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh

All present enzymatic activity of Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh:
3.2.1.52;

The structure of Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh, PDB code: 4az7 was solved by B.Pluvinage, K.A.Stubbs, D.J.Vocadlo, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.12 / 1.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.500, 109.800, 112.500, 90.00, 90.00, 90.00
R / Rfree (%)	14.203 / 17.221

The binding sites of Magnesium atom in the Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh (pdb code 4az7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh, PDB code: 4az7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1617 b:17.7 occ:1.00 OD2 A:ASP259 2.1 16.9 1.0 O A:HOH2134 2.1 16.8 1.0 O A:HOH2135 2.1 16.4 1.0 O A:HOH2579 2.1 21.7 1.0 O A:HOH2132 2.1 18.7 1.0 O A:HOH2133 2.1 19.7 1.0 CG A:ASP259 3.1 16.7 1.0 OD1 A:ASP259 3.5 16.9 1.0 O A:HOH2203 4.0 18.1 1.0 ND2 A:ASN303 4.1 10.6 1.0 OD1 A:ASN303 4.1 12.1 1.0 O A:ASP259 4.2 12.9 1.0 O A:HOH2150 4.2 22.3 1.0 O A:HOH2202 4.3 15.4 1.0 CB A:ASP259 4.4 14.2 1.0 O A:HOH2209 4.5 31.9 1.0 CG A:ASN303 4.5 11.5 1.0 C A:ASP259 4.6 13.0 1.0 O A:HOH2205 4.7 15.2 1.0 O A:HOH2149 4.9 39.2 1.0

Magnesium binding site 2 out of 2 in the Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Differential Inhibition of the Tandem GH20 Catalytic Modules in the Pneumococcal Exo-Beta-D-N-Acetylglucosaminidase, Strh within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1622 b:39.4 occ:1.00 O A:HOH2583 2.1 38.8 1.0 O A:HOH2582 2.1 30.9 1.0 O A:HOH2581 2.1 34.3 1.0 O A:HOH2501 2.1 16.8 1.0 O A:HOH2502 2.2 27.0 1.0 O A:HOH2498 3.8 29.6 1.0 O A:ASN557 4.3 14.1 1.0 O A:HOH2499 4.3 35.9 1.0 CA A:ASN557 4.7 15.1 1.0 OD1 A:ASN557 4.8 20.8 1.0 C A:ASN557 5.0 14.8 1.0

B.Pluvinage, K.A.Stubbs, D.J.Vocadlo, A.B.Boraston. Inhibition of the Family 20 Glycoside Hydrolase Catalytic Modules in the Streptococcus Pneumoniae Exo-Beta-D-N- Acetylglucosaminidase, Strh. Org.Biomol.Chem. V. 11 7907 2013.
ISSN: ISSN 1477-0520
PubMed: 24132305
DOI: 10.1039/C3OB41579A