Calcium in PDB 1cxi: Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55

All present enzymatic activity of Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55:
2.4.1.19;

The structure of Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55, PDB code: 1cxi was solved by R.M.A.Knegtel, B.V.Strokopytov, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	117.950, 109.800, 65.650, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55 (pdb code 1cxi). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55, PDB code: 1cxi:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca690 b:16.9 occ:1.00 OD1 A:ASN33 2.3 21.5 1.0 OD1 A:ASP27 2.4 15.5 1.0 OD1 A:ASN32 2.4 11.7 1.0 OD2 A:ASP53 2.4 17.6 1.0 O A:HOH872 2.5 15.3 1.0 O A:ASN29 2.6 17.2 1.0 O A:GLY51 2.7 16.0 1.0 CG A:ASP27 3.4 16.6 1.0 CG A:ASP53 3.4 15.2 1.0 C A:ASN29 3.4 16.8 1.0 CG A:ASN33 3.5 24.4 1.0 CG A:ASN32 3.6 17.9 1.0 C A:GLY51 3.7 15.8 1.0 CB A:ASP53 3.9 8.5 1.0 OD2 A:ASP27 4.0 18.4 1.0 N A:ASN33 4.0 13.2 1.0 N A:PRO30 4.1 12.9 1.0 CA A:GLY51 4.1 11.4 1.0 CA A:PRO30 4.2 12.2 1.0 N A:ASN29 4.2 12.3 1.0 ND2 A:ASN32 4.2 6.8 1.0 CA A:ASN33 4.3 13.4 1.0 CA A:ASN29 4.3 12.3 1.0 O A:ALA111 4.3 10.8 1.0 C A:ASN32 4.3 15.3 1.0 ND2 A:ASN33 4.3 12.3 1.0 CB A:ASP27 4.4 9.9 1.0 OD1 A:ASP53 4.4 15.7 1.0 CA A:ASP27 4.5 8.3 1.0 CB A:ASN33 4.5 13.3 1.0 C A:PRO30 4.5 17.1 1.0 N A:ASN32 4.6 13.0 1.0 CB A:ASN29 4.6 12.2 1.0 O A:PRO30 4.6 17.6 1.0 CB A:ASN32 4.7 12.3 1.0 CA A:ASN32 4.7 11.8 1.0 N A:ASP53 4.8 7.2 1.0 O A:ASN32 4.8 15.9 1.0 C A:GLY52 4.8 11.5 1.0 N A:GLY52 4.8 11.5 1.0 C A:ASP27 4.9 14.7 1.0 N A:GLY28 5.0 11.2 1.0 O A:HOH874 5.0 8.0 1.0 CA A:ASP53 5.0 7.3 1.0

Calcium binding site 2 out of 2 in the Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Wild-Type Cgtase From Bacillus Circulans Strain 251 at 120 K and pH 7.55 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca691 b:6.2 occ:1.00 OD1 A:ASN139 2.4 13.1 1.0 O A:HIS233 2.4 7.0 1.0 O A:HOH866 2.4 4.0 1.0 O A:HOH897 2.4 5.5 1.0 OD1 A:ASP199 2.4 9.8 1.0 O A:HOH893 2.4 2.8 1.0 O A:ILE190 2.6 11.2 1.0 OD2 A:ASP199 2.7 12.9 1.0 CG A:ASP199 2.9 8.4 1.0 CG A:ASN139 3.4 19.1 1.0 C A:HIS233 3.6 7.3 1.0 C A:ILE190 3.7 10.1 1.0 ND2 A:ASN139 3.9 8.5 1.0 O A:ASN139 4.2 13.4 1.0 CA A:ILE190 4.3 3.8 1.0 CB A:HIS233 4.3 5.0 1.0 CB A:ASP199 4.4 7.1 1.0 CA A:MET234 4.4 1.6 1.0 N A:MET234 4.4 3.5 1.0 O A:GLY189 4.5 7.8 1.0 CA A:HIS233 4.5 4.4 1.0 O A:LYS192 4.5 13.1 1.0 CG A:MET234 4.6 6.0 1.0 O A:HOH925 4.6 13.2 1.0 CB A:ASN139 4.7 6.5 1.0 N A:TYR191 4.8 7.4 1.0 O A:LEU200 4.9 11.2 1.0 ND1 A:HIS176 4.9 13.1 1.0 CG2 A:ILE190 4.9 4.8 1.0

R.M.Knegtel, B.Strokopytov, D.Penninga, O.G.Faber, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, B.W.Dijkstra. Crystallographic Studies of the Interaction of Cyclodextrin Glycosyltransferase From Bacillus Circulans Strain 251 with Natural Substrates and Products. J.Biol.Chem. V. 270 29256 1995.
ISSN: ISSN 0021-9258
PubMed: 7493956
DOI: 10.1074/JBC.270.49.29256