Calcium in PDB 1eo5: Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose

All present enzymatic activity of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose:
2.4.1.19;

The structure of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose, PDB code: 1eo5 was solved by J.C.M.Uitdehaag, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	116.700, 109.700, 67.500, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 21

The binding sites of Calcium atom in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose (pdb code 1eo5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose, PDB code: 1eo5:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose


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 in Complex with Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca688 b:16.7 occ:1.00 OD1 A:ASN33 2.1 18.5 1.0 OD2 A:ASP53 2.3 18.3 1.0 OD1 A:ASN32 2.3 12.8 1.0 O A:HOH954 2.3 13.8 1.0 OD1 A:ASP27 2.5 26.0 1.0 O A:GLY51 2.5 14.2 1.0 O A:ASN29 2.6 18.7 1.0 CG A:ASP27 3.3 24.8 1.0 CG A:ASN33 3.3 22.6 1.0 CG A:ASP53 3.3 18.3 1.0 C A:ASN29 3.3 20.8 1.0 CG A:ASN32 3.4 25.1 1.0 C A:GLY51 3.5 16.3 1.0 OD2 A:ASP27 3.8 25.4 1.0 CB A:ASP53 3.8 15.1 1.0 N A:ASN33 3.9 16.6 1.0 CA A:GLY51 4.0 13.9 1.0 ND2 A:ASN32 4.0 15.8 1.0 N A:PRO30 4.1 20.1 1.0 ND2 A:ASN33 4.1 15.5 1.0 N A:ASN29 4.1 17.7 1.0 CA A:PRO30 4.2 19.8 1.0 CA A:ASN29 4.2 17.0 1.0 O A:ALA111 4.2 15.6 1.0 CA A:ASN33 4.2 15.9 1.0 CB A:ASP27 4.2 18.2 1.0 C A:ASN32 4.3 20.5 1.0 OD1 A:ASP53 4.4 14.5 1.0 CB A:ASN33 4.4 16.9 1.0 CA A:ASP27 4.4 16.2 1.0 C A:PRO30 4.6 21.6 1.0 CB A:ASN29 4.6 17.7 1.0 N A:ASN32 4.6 17.6 1.0 CB A:ASN32 4.6 13.6 1.0 CA A:ASN32 4.7 16.6 1.0 N A:GLY52 4.7 12.2 1.0 C A:GLY52 4.7 16.4 1.0 O A:PRO30 4.8 21.1 1.0 N A:ASP53 4.8 12.7 1.0 C A:ASP27 4.8 22.4 1.0 O A:ASN32 4.8 21.2 1.0 O A:HOH830 4.8 19.1 1.0 O A:GLY52 4.8 17.6 1.0 N A:GLY28 4.9 18.1 1.0 CA A:ASP53 4.9 12.8 1.0

Calcium binding site 2 out of 3 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose


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 in Complex with Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca689 b:13.5 occ:1.00 O A:HIS233 2.3 14.6 1.0 O A:HOH1004 2.4 15.3 1.0 O A:HOH1000 2.4 11.5 1.0 OD2 A:ASP199 2.4 16.9 1.0 O A:HOH1020 2.5 15.1 1.0 OD1 A:ASN139 2.5 13.0 1.0 OD1 A:ASP199 2.5 11.0 1.0 O A:ILE190 2.7 13.6 1.0 CG A:ASP199 2.8 11.9 1.0 CG A:ASN139 3.5 16.1 1.0 C A:HIS233 3.6 16.0 1.0 C A:ILE190 3.8 14.5 1.0 ND2 A:ASN139 4.0 11.7 1.0 O A:ASN139 4.3 15.3 1.0 CB A:ASP199 4.3 10.1 1.0 CA A:ILE190 4.4 9.8 1.0 O A:LYS192 4.4 15.2 1.0 CB A:HIS233 4.4 14.2 1.0 N A:MET234 4.4 10.5 1.0 CA A:MET234 4.5 9.5 1.0 CA A:HIS233 4.5 13.0 1.0 O A:GLY189 4.6 13.3 1.0 O A:HOH754 4.6 11.8 1.0 CG A:MET234 4.7 13.2 1.0 ND1 A:HIS176 4.7 16.9 1.0 O A:LEU200 4.7 12.8 1.0 CB A:ASN139 4.8 11.3 1.0 CG2 A:ILE190 4.8 10.6 1.0 N A:TYR191 4.9 12.5 1.0 O A:HOH762 4.9 12.7 1.0 CE1 A:HIS176 5.0 17.2 1.0

Calcium binding site 3 out of 3 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Bacillus Circulans Strain 251 Cyclodextrin Glycosyltransferase in Complex with Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca690 b:28.0 occ:1.00 O A:HOH1014 2.2 13.1 1.0 O A:HOH1164 2.3 33.2 1.0 O A:ALA315 2.3 16.1 1.0 O A:HOH913 2.5 31.3 1.0 OD1 A:ASP577 2.6 23.1 1.0 O A:HOH1155 2.7 31.5 1.0 O A:HOH967 2.8 19.7 1.0 C A:ALA315 3.4 15.7 1.0 CG A:ASP577 3.7 26.3 1.0 CA A:ALA315 4.1 9.8 1.0 OD2 A:ASP577 4.1 36.7 1.0 NE2 A:GLN316 4.2 11.6 1.0 O A:HOH758 4.3 15.6 1.0 O A:ASP577 4.4 13.2 1.0 N A:GLN316 4.5 10.8 1.0 CB A:ALA315 4.5 10.1 1.0 O A:HOH1178 4.5 29.5 1.0 N A:ASP577 4.6 12.6 1.0 O A:HOH1229 4.7 42.5 1.0 O A:HOH1066 4.8 24.5 1.0 O A:HOH831 4.8 16.0 1.0 CG A:GLN316 4.8 8.7 1.0 CA A:GLN316 4.8 10.0 1.0 C A:ASP577 4.8 15.8 1.0 CB A:ASP577 4.9 13.6 1.0 CA A:ASP577 5.0 11.2 1.0

J.C.Uitdehaag, G.J.Van Alebeek, B.A.Van Der Veen, L.Dijkhuizen, B.W.Dijkstra. Structures of Maltohexaose and Maltoheptaose Bound at the Donor Sites of Cyclodextrin Glycosyltransferase Give Insight Into the Mechanisms of Transglycosylation Activity and Cyclodextrin Size Specificity. Biochemistry V. 39 7772 2000.
ISSN: ISSN 0006-2960
PubMed: 10869182
DOI: 10.1021/BI000340X