Calcium in PDB 2ces: Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole

All present enzymatic activity of Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole:
3.2.1.21;

The structure of Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole, PDB code: 2ces was solved by T.M.Gloster, S.Roberts, A.Vasella, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.55 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	94.483, 94.886, 113.928, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 24.7

The binding sites of Calcium atom in the Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole (pdb code 2ces). 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 Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole, PDB code: 2ces:

Calcium binding site 1 out of 1 in the Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Beta-Glucosidase From Thermotoga Maritima in Complex with Glucoimidazole within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1445 b:72.5 occ:1.00 O B:HOH2168 1.8 6.5 0.5 O B:ASP278 2.5 34.1 1.0 O B:HOH2164 3.0 38.0 1.0 O B:HOH2166 3.2 56.5 1.0 OE2 B:GLU282 3.2 50.4 1.0 C B:ASP278 3.5 34.0 1.0 CB B:SER281 3.7 40.0 1.0 O B:HOH2165 4.0 48.8 1.0 CA B:ASP278 4.0 33.3 1.0 OG B:SER281 4.2 43.4 1.0 CD B:GLU282 4.3 49.5 1.0 CB B:ASP278 4.6 34.1 1.0 N B:SER281 4.6 37.0 1.0 N B:ASP279 4.6 32.9 1.0 CA B:SER281 4.8 39.0 1.0 CA B:ASP279 4.9 32.2 1.0

T.M.Gloster, S.Roberts, G.Perugino, M.Rossi, M.Moracci, N.Panday, M.Terinek, A.Vasella, G.J.Davies. Structural, Kinetic, and Thermodynamic Analysis of Glucoimidazole-Derived Glycosidase Inhibitors. Biochemistry V. 45 11879 2006.
ISSN: ISSN 0006-2960
PubMed: 17002288
DOI: 10.1021/BI060973X