Calcium in PDB 2j75: Beta-Glucosidase From Thermotoga Maritima in Complex with Noeuromycin

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

The structure of Beta-Glucosidase From Thermotoga Maritima in Complex with Noeuromycin, PDB code: 2j75 was solved by T.M.Gloster, P.Meloncelli, R.V.Stick, D.Zechel, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.55 / 1.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	93.923, 94.326, 113.048, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 24.3

The binding sites of Calcium atom in the Beta-Glucosidase From Thermotoga Maritima in Complex with Noeuromycin (pdb code 2j75). 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 Noeuromycin, PDB code: 2j75:

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


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 Noeuromycin within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1446 b:33.9 occ:1.00 O B:HOH2245 2.0 34.0 1.0 OE1 B:GLU282 2.3 20.1 0.5 O B:ASP278 2.5 21.2 1.0 OE2 B:GLU282 2.6 19.9 0.5 O B:HOH2239 2.6 48.0 1.0 CD B:GLU282 2.8 21.3 0.5 OG B:SER281 3.3 27.2 0.5 C B:ASP278 3.6 22.0 1.0 CG B:GLU282 4.3 22.9 0.5 O B:HOH2235 4.4 25.6 1.0 CA B:ASP279 4.5 20.2 1.0 N B:ASP279 4.5 21.0 1.0 CA B:ASP278 4.6 21.8 1.0 CB B:SER281 4.6 25.5 0.5 CB B:SER281 4.6 25.1 0.5 O B:HOH2248 4.7 26.8 1.0 O B:HOH2241 4.8 40.1 1.0 OE2 B:GLU282 4.8 31.1 0.5 CB B:ASP278 4.8 21.7 1.0 CG B:GLU282 4.9 26.7 0.5 C B:ASP279 5.0 20.1 1.0

T.M.Gloster, P.Meloncelli, R.V.Stick, D.Zechel, A.Vasella, G.J.Davies. Glycosidase Inhibition: An Assessment of the Binding of 18 Putative Transition-State Mimics. J.Am.Chem.Soc. V. 129 2345 2007.
ISSN: ISSN 0002-7863
PubMed: 17279749
DOI: 10.1021/JA066961G