Calcium in PDB 4aie: Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm

All present enzymatic activity of Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm:
3.2.1.10; 3.2.1.70;

The structure of Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm, PDB code: 4aie was solved by F.Fredslund, J.C.Navarro Poulsen, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.42 / 2.05
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	55.830, 107.250, 103.610, 90.00, 90.00, 90.00
R / Rfree (%)	13.7 / 18.3

The binding sites of Calcium atom in the Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm (pdb code 4aie). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm, PDB code: 4aie:

Calcium binding site 1 out of 1 in the Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1540 b:26.5 occ:1.00 O A:HOH2030 2.4 25.2 1.0 O A:ILE26 2.4 17.4 1.0 OD2 A:ASP28 2.4 15.6 1.0 OD1 A:ASN22 2.5 21.6 1.0 OD1 A:ASP20 2.5 17.5 1.0 OD1 A:ASP24 2.5 19.0 1.0 CG A:ASP24 3.2 19.6 1.0 HB3 A:ASP28 3.2 19.0 1.0 OD2 A:ASP24 3.3 22.1 1.0 H A:ASN22 3.3 25.6 1.0 HA A:ASP20 3.4 15.9 1.0 CG A:ASP20 3.4 18.7 1.0 H A:SER21 3.4 26.0 1.0 H A:ILE26 3.4 20.3 1.0 CG A:ASP28 3.5 14.9 1.0 CG A:ASN22 3.5 31.4 1.0 H A:ASP24 3.5 21.4 1.0 C A:ILE26 3.5 15.4 1.0 HB A:ILE26 3.6 19.8 1.0 CB A:ASP28 3.8 15.9 1.0 HD22 A:ASN22 3.9 48.6 1.0 CA A:ASP20 4.1 13.2 1.0 ND2 A:ASN22 4.1 40.5 1.0 N A:ILE26 4.1 16.9 1.0 N A:SER21 4.1 21.7 1.0 N A:ASN22 4.1 21.3 1.0 CB A:ASP20 4.2 15.6 1.0 OD2 A:ASP20 4.2 19.7 1.0 CA A:ILE26 4.2 17.9 1.0 HB2 A:ASP20 4.3 18.7 1.0 H A:GLY23 4.3 28.2 1.0 CB A:ILE26 4.3 16.5 1.0 N A:ASP24 4.3 17.8 1.0 HA2 A:GLY27 4.4 18.0 1.0 C A:GLY27 4.4 11.1 1.0 CB A:ASP24 4.5 20.7 1.0 HG22 A:ILE26 4.5 26.1 1.0 N A:ASP28 4.5 13.2 1.0 O A:GLN73 4.5 18.8 1.0 HB2 A:ASP28 4.5 19.0 1.0 H A:GLY25 4.6 23.2 1.0 N A:GLY27 4.6 16.1 1.0 OD1 A:ASP28 4.6 17.7 1.0 CB A:ASN22 4.6 22.8 1.0 C A:ASP20 4.6 17.9 1.0 N A:GLY23 4.6 23.5 1.0 CA A:ASN22 4.7 20.9 1.0 CA A:GLY27 4.7 15.0 1.0 O A:GLY27 4.7 12.3 1.0 H A:ASP28 4.7 15.8 1.0 HG A:SER21 4.8 22.2 1.0 HB3 A:ASP24 4.8 24.9 1.0 HB3 A:ASN22 4.8 27.3 1.0 C A:ASN22 4.8 25.9 1.0 CA A:ASP24 4.8 17.9 1.0 CA A:ASP28 4.8 11.9 1.0 N A:GLY25 4.8 19.3 1.0 HD21 A:ASN22 4.9 48.6 1.0 CG2 A:ILE26 4.9 21.8 1.0

M.S.Moller, F.Fredslund, A.Majumder, H.Nakai, J.N.Poulsen, L.Lo Leggio, B.Svensson, M.Abou Hachem. Enzymology and Structure of the GH13_31 Glucan 1,6-Alpha-Glucosidase That Confers Isomaltooligosaccharide Utilization in the Probiotic Lactobacillus Acidophilus Ncfm. J.Bacteriol. V. 194 4249 2012.
ISSN: ISSN 0021-9193
PubMed: 22685275
DOI: 10.1128/JB.00622-12