Calcium in PDB 1dtu: Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor

All present enzymatic activity of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor:
2.4.1.19;

The structure of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor, PDB code: 1dtu was solved by J.C.M.Uitdehaag, K.H.Kalk, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	120.445, 111.160, 65.758, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 24.8

The binding sites of Calcium atom in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor (pdb code 1dtu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor, PDB code: 1dtu:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca687 b:24.3 occ:1.00 OD1 A:ASN33 2.2 48.8 1.0 OD1 A:ASP27 2.3 28.3 1.0 O A:HOH754 2.4 13.6 1.0 OD1 A:ASN32 2.4 26.1 1.0 OD2 A:ASP53 2.5 25.4 1.0 O A:GLY51 2.5 28.9 1.0 O A:ASN29 2.6 26.9 1.0 CG A:ASP27 3.3 26.4 1.0 CG A:ASN33 3.3 46.9 1.0 C A:ASN29 3.5 28.6 1.0 CG A:ASP53 3.5 28.3 1.0 C A:GLY51 3.6 28.0 1.0 CG A:ASN32 3.6 30.6 1.0 CB A:ASP53 3.8 21.6 1.0 CA A:GLY51 4.0 22.7 1.0 ND2 A:ASN33 4.1 32.6 1.0 OD2 A:ASP27 4.1 26.9 1.0 N A:ASN33 4.2 22.6 1.0 ND2 A:ASN32 4.2 18.2 1.0 N A:PRO30 4.2 26.0 1.0 O A:ALA111 4.3 20.3 1.0 CA A:PRO30 4.3 26.0 1.0 CB A:ASP27 4.3 22.2 1.0 N A:ASN29 4.3 23.1 1.0 CA A:ASN33 4.4 22.6 1.0 C A:ASN32 4.4 26.7 1.0 CA A:ASN29 4.4 23.1 1.0 CB A:ASN33 4.4 17.9 1.0 CA A:ASP27 4.5 20.4 1.0 OD1 A:ASP53 4.6 33.2 1.0 C A:GLY52 4.7 25.7 1.0 O A:ASN32 4.7 27.4 1.0 O A:GLY52 4.7 25.5 1.0 C A:PRO30 4.7 30.2 1.0 N A:GLY52 4.7 23.4 1.0 N A:ASN32 4.8 24.2 1.0 O A:HOH763 4.8 20.6 1.0 CB A:ASN32 4.8 20.5 1.0 N A:ASP53 4.8 21.3 1.0 CA A:ASN32 4.9 22.5 1.0 C A:ASP27 4.9 26.5 1.0 CB A:ASN29 4.9 22.9 1.0 CA A:ASP53 5.0 20.7 1.0

Calcium binding site 2 out of 2 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase: A Mutant Y89D/S146P Complexed to An Hexasaccharide Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca688 b:15.1 occ:1.00 O A:HIS233 2.3 15.8 1.0 OD1 A:ASN139 2.4 20.1 1.0 O A:HOH862 2.4 18.0 1.0 O A:HOH768 2.5 7.0 1.0 OD1 A:ASP199 2.5 17.2 1.0 O A:ILE190 2.6 16.3 1.0 O A:HOH743 2.6 16.2 1.0 OD2 A:ASP199 2.7 15.6 1.0 CG A:ASP199 2.9 17.4 1.0 CG A:ASN139 3.5 21.1 1.0 C A:HIS233 3.6 13.4 1.0 C A:ILE190 3.8 17.2 1.0 ND2 A:ASN139 4.1 15.3 1.0 O A:ASN139 4.3 19.4 1.0 CB A:HIS233 4.3 11.0 1.0 CA A:ILE190 4.4 11.6 1.0 CB A:ASP199 4.4 16.2 1.0 O A:LYS192 4.4 18.7 1.0 N A:MET234 4.5 7.7 1.0 CA A:HIS233 4.5 10.0 1.0 CA A:MET234 4.5 6.7 1.0 O A:GLY189 4.6 18.6 1.0 CG A:MET234 4.7 13.1 1.0 CB A:ASN139 4.7 9.8 1.0 O A:LEU200 4.8 16.6 1.0 N A:TYR191 4.8 14.3 1.0 ND1 A:HIS176 4.9 20.0 1.0 O A:HOH746 4.9 21.5 1.0 O A:HOH731 4.9 12.1 1.0 CG2 A:ILE190 5.0 11.0 1.0

B.A.Van Der Veen, J.C.Uitdehaag, D.Penninga, G.J.Van Alebeek, L.M.Smith, B.W.Dijkstra, L.Dijkhuizen. Rational Design of Cyclodextrin Glycosyltransferase From Bacillus Circulans Strain 251 to Increase Alpha-Cyclodextrin Production. J.Mol.Biol. V. 296 1027 2000.
ISSN: ISSN 0022-2836
PubMed: 10686101
DOI: 10.1006/JMBI.2000.3528