Magnesium in PDB 3wy4: Crystal Structure of Alpha-Glucosidase Mutant E271Q in Complex with Maltose

All present enzymatic activity of Crystal Structure of Alpha-Glucosidase Mutant E271Q in Complex with Maltose:
3.2.1.20;

The structure of Crystal Structure of Alpha-Glucosidase Mutant E271Q in Complex with Maltose, PDB code: 3wy4 was solved by X.Shen, Z.Gai, K.Kato, M.Yao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.46 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.464, 181.062, 51.933, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 24.1

The binding sites of Magnesium atom in the Crystal Structure of Alpha-Glucosidase Mutant E271Q in Complex with Maltose (pdb code 3wy4). 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 Alpha-Glucosidase Mutant E271Q in Complex with Maltose, PDB code: 3wy4:

Magnesium binding site 1 out of 1 in the Crystal Structure of Alpha-Glucosidase Mutant E271Q in Complex with Maltose


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 Alpha-Glucosidase Mutant E271Q in Complex with Maltose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg600 b:39.6 occ:1.00 O A:VAL29 2.1 32.3 1.0 O A:HOH729 2.1 32.2 1.0 OD1 A:ASP23 2.4 33.8 1.0 OD2 A:ASP31 2.4 32.5 1.0 OD1 A:ASP27 2.6 29.6 1.0 C A:VAL29 3.3 34.2 1.0 CG A:ASP31 3.3 32.5 1.0 CG A:ASP23 3.4 35.7 1.0 CG A:ASP27 3.5 38.5 1.0 CB A:ASP31 3.6 32.7 1.0 OD2 A:ASP27 3.8 41.7 1.0 CB A:ARG25 3.8 37.8 1.0 C A:GLY30 3.9 31.6 1.0 N A:ASP31 3.9 28.0 1.0 CB A:ASP23 4.0 29.4 1.0 CA A:ASP23 4.0 31.4 1.0 N A:ARG25 4.0 34.0 1.0 CG A:ARG25 4.0 39.2 1.0 N A:SER24 4.2 30.7 1.0 O A:GLY30 4.2 29.5 1.0 N A:GLY30 4.2 34.4 1.0 CA A:GLY30 4.2 26.1 1.0 CA A:VAL29 4.3 32.7 1.0 N A:VAL29 4.3 30.2 1.0 CA A:ASP31 4.4 33.1 1.0 OD2 A:ASP23 4.4 38.1 1.0 CA A:ARG25 4.4 36.4 1.0 OD1 A:ASP31 4.5 34.3 1.0 C A:ASP23 4.5 33.0 1.0 O A:MET76 4.5 52.1 1.0 CB A:VAL29 4.6 35.5 1.0 N A:ASP27 4.8 39.0 1.0 N A:GLY26 4.8 36.1 1.0 C A:ARG25 4.9 39.3 1.0 CB A:ASP27 4.9 40.8 1.0

X.Shen, W.Saburi, Z.Gai, K.Kato, T.Ojima-Kato, J.Yu, K.Komoda, Y.Kido, H.Matsui, H.Mori, M.Yao. Structural Analysis of the Alpha-Glucosidase Hag Provides New Insights Into Substrate Specificity and Catalytic Mechanism Acta Crystallogr. D Biol. V. 71 1382 2015CRYSTALLOGR..
ISSN: ESSN 1399-0047
PubMed: 26057678
DOI: 10.1107/S139900471500721X