Calcium in PDB 1ot1: Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A

All present enzymatic activity of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A:
2.4.1.19;

The structure of Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A, PDB code: 1ot1 was solved by H.J.Rozeboom, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.90 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	116.940, 109.765, 67.750, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18.1

The binding sites of Calcium atom in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A (pdb code 1ot1). 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 Glycosyl Transferase Mutant D135A, PDB code: 1ot1:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A


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 Glycosyl Transferase Mutant D135A within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1692 b:18.9 occ:1.00 OD1 A:ASN33 2.2 20.4 1.0 OD2 A:ASP53 2.3 19.8 1.0 OD1 A:ASN32 2.3 19.1 1.0 OD1 A:ASP27 2.4 19.8 1.0 O A:HOH2488 2.5 18.4 1.0 O A:ASN29 2.5 19.8 1.0 O A:GLY51 2.6 18.1 1.0 CG A:ASP53 3.3 17.9 1.0 CG A:ASP27 3.4 21.0 1.0 C A:ASN29 3.4 20.4 1.0 CG A:ASN33 3.4 21.1 1.0 CG A:ASN32 3.4 20.7 1.0 C A:GLY51 3.6 17.2 1.0 CB A:ASP53 3.8 17.0 1.0 ND2 A:ASN32 4.0 21.4 1.0 OD2 A:ASP27 4.0 20.2 1.0 N A:ASN33 4.1 21.9 1.0 CA A:GLY51 4.1 17.6 1.0 N A:ASN29 4.2 20.3 1.0 N A:PRO30 4.2 21.9 1.0 ND2 A:ASN33 4.2 20.8 1.0 CA A:ASN29 4.2 20.7 1.0 O A:ALA111 4.2 18.5 1.0 CA A:PRO30 4.3 21.4 1.0 CA A:ASN33 4.3 22.2 1.0 OD1 A:ASP53 4.3 15.8 1.0 CB A:ASP27 4.4 20.3 1.0 C A:ASN32 4.4 21.4 1.0 CB A:ASN33 4.5 21.7 1.0 CA A:ASP27 4.5 19.1 1.0 CB A:ASN29 4.6 20.6 1.0 C A:PRO30 4.6 21.0 1.0 N A:ASN32 4.7 21.5 1.0 CB A:ASN32 4.7 21.2 1.0 N A:ASP53 4.7 16.5 1.0 C A:GLY52 4.8 16.6 1.0 O A:HOH1784 4.8 21.1 1.0 CA A:ASN32 4.8 21.5 1.0 N A:GLY52 4.8 16.2 1.0 C A:ASP27 4.8 20.0 1.0 O A:ASN32 4.9 21.7 1.0 O A:PRO30 4.9 21.2 1.0 N A:GLY28 4.9 18.7 1.0 CA A:ASP53 4.9 17.2 1.0 O A:GLY52 5.0 17.6 1.0

Calcium binding site 2 out of 3 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A


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 Glycosyl Transferase Mutant D135A within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1693 b:15.8 occ:1.00 O A:HIS233 2.4 14.2 1.0 OD1 A:ASN139 2.4 16.1 1.0 O A:HOH1735 2.4 16.6 1.0 O A:HOH2489 2.4 17.6 1.0 O A:HOH1734 2.5 14.4 1.0 OD2 A:ASP199 2.5 13.6 1.0 O A:ILE190 2.5 15.7 1.0 OD1 A:ASP199 2.5 13.4 1.0 CG A:ASP199 2.9 14.4 1.0 CG A:ASN139 3.5 15.8 1.0 C A:HIS233 3.6 15.2 1.0 C A:ILE190 3.7 16.0 1.0 ND2 A:ASN139 4.0 14.9 1.0 CA A:ILE190 4.2 14.9 1.0 O A:ASN139 4.3 13.9 1.0 CB A:ASP199 4.4 14.9 1.0 CA A:MET234 4.4 13.3 1.0 O A:LYS192 4.4 17.9 1.0 N A:MET234 4.4 12.8 1.0 CB A:HIS233 4.5 16.0 1.0 O A:GLY189 4.5 15.7 1.0 CA A:HIS233 4.6 14.8 1.0 O A:HOH1729 4.6 14.9 1.0 CG A:MET234 4.6 13.4 1.0 ND1 A:HIS176 4.7 17.2 1.0 CG2 A:ILE190 4.7 14.0 1.0 CB A:ASN139 4.8 13.0 1.0 N A:TYR191 4.8 17.1 1.0 O A:LEU200 4.8 15.9 1.0

Calcium binding site 3 out of 3 in the Bacillus Circulans Strain 251 Cyclodextrin Glycosyl Transferase Mutant D135A


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 Glycosyl Transferase Mutant D135A within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1694 b:25.6 occ:1.00 O A:ALA315 2.3 13.4 1.0 O A:HOH2066 2.4 30.7 1.0 O A:HOH1894 2.4 31.5 1.0 O A:HOH1788 2.4 15.3 1.0 O A:HOH2109 2.4 26.2 1.0 OD1 A:ASP577 2.6 25.5 1.0 O A:HOH1996 2.6 27.2 1.0 C A:ALA315 3.5 12.8 1.0 CG A:ASP577 3.7 23.9 1.0 OD2 A:ASP577 4.1 27.1 1.0 CA A:ALA315 4.1 13.6 1.0 O A:HOH1810 4.2 15.4 1.0 O A:HOH2286 4.2 39.8 1.0 O A:HOH2399 4.5 44.4 1.0 OE1 A:GLN316 4.5 12.5 1.0 N A:GLN316 4.5 11.8 1.0 CB A:ALA315 4.6 13.9 1.0 O A:ASP577 4.6 14.9 1.0 O A:HOH2110 4.6 26.9 1.0 O A:HOH2059 4.6 21.2 1.0 N A:ASP577 4.6 16.0 1.0 CA A:GLN316 4.8 12.0 1.0 O A:HOH1783 4.8 16.3 1.0 CG A:GLN316 4.9 12.2 1.0 C A:ASP577 4.9 16.5 1.0 CB A:ASP577 5.0 20.4 1.0

H.Leemhuis, H.J.Rozeboom, B.W.Dijkstra, L.Dijkhuizen. The Fully Conserved Asp Residue in Conserved Sequence Region I of the Alpha-Amylase Family Is Crucial For the Catalytic Site Architecture and Activity Febs Lett. V. 541 47 2003.
ISSN: ISSN 0014-5793
PubMed: 12706817
DOI: 10.1016/S0014-5793(03)00286-2