Calcium in PDB 1a47: Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor

All present enzymatic activity of Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor:
2.4.1.19;

The structure of Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor, PDB code: 1a47 was solved by J.C.M.Uitdehaag, K.H.Kalk, 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)	8.00 / 2.56
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.996, 97.789, 116.263, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 25.4

The binding sites of Calcium atom in the Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor (pdb code 1a47). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor, PDB code: 1a47:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca685 b:18.8 occ:1.00 OD1 A:ASN140 2.3 26.6 1.0 O A:HOH882 2.4 23.4 1.0 O A:HIS234 2.4 13.1 1.0 O A:ILE191 2.5 10.6 1.0 OD1 A:ASP200 2.5 15.1 1.0 O A:HOH839 2.6 13.8 1.0 OD2 A:ASP200 2.6 18.6 1.0 O A:HOH838 2.7 11.3 1.0 CG A:ASP200 2.9 14.9 1.0 CG A:ASN140 3.4 19.2 1.0 C A:ILE191 3.6 12.0 1.0 C A:HIS234 3.6 12.4 1.0 ND2 A:ASN140 3.8 6.8 1.0 O A:ARG193 4.3 14.8 1.0 CA A:ILE191 4.3 6.2 1.0 O A:ASN140 4.3 10.1 1.0 CB A:HIS234 4.3 9.1 1.0 OE1 A:GLN203 4.4 9.9 1.0 CB A:ASP200 4.4 8.8 1.0 CG A:MET235 4.5 14.4 1.0 CA A:HIS234 4.5 8.1 1.0 O A:GLY190 4.5 12.4 1.0 N A:MET235 4.5 9.0 1.0 CA A:MET235 4.6 9.6 1.0 CB A:ASN140 4.7 10.0 1.0 N A:TYR192 4.7 9.9 1.0 ND1 A:HIS177 4.9 14.4 1.0 O A:LEU201 4.9 16.7 1.0 CG2 A:ILE191 4.9 10.2 1.0

Calcium binding site 2 out of 2 in the Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cgtase From Thermoanaerobacterium Thermosulfurigenes EM1 in Complex with A Maltohexaose Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca686 b:11.6 occ:1.00 OD1 A:ASN33 2.1 26.4 1.0 OD2 A:ASP53 2.1 20.6 1.0 O A:ASN29 2.3 16.4 1.0 OD1 A:ASN32 2.4 9.7 1.0 O A:HOH840 2.5 18.6 1.0 OD1 A:ASP27 2.5 19.7 1.0 O A:GLY51 2.5 11.8 1.0 CG A:ASN33 3.3 24.6 1.0 CG A:ASP27 3.3 19.6 1.0 CG A:ASP53 3.4 15.5 1.0 C A:ASN29 3.4 17.6 1.0 C A:GLY51 3.5 12.3 1.0 CG A:ASN32 3.6 16.3 1.0 CA A:GLY51 3.8 8.7 1.0 OD2 A:ASP27 3.9 21.7 1.0 N A:ASN33 4.0 17.4 1.0 CB A:ASP53 4.0 12.4 1.0 ND2 A:ASN33 4.0 21.7 1.0 ND2 A:ASN32 4.2 5.0 1.0 CA A:ASN33 4.2 16.2 1.0 N A:THR30 4.3 16.2 1.0 N A:ASN29 4.3 14.1 1.0 CA A:THR30 4.3 17.1 1.0 OD1 A:ASP53 4.3 13.6 1.0 CB A:ASN33 4.3 9.1 1.0 CB A:ASP27 4.3 11.6 1.0 CA A:ASN29 4.4 13.8 1.0 O A:TYR112 4.4 10.9 1.0 C A:ASN32 4.4 19.7 1.0 CA A:ASP27 4.5 11.0 1.0 N A:GLY52 4.7 9.6 1.0 C A:GLY52 4.8 16.4 1.0 C A:THR30 4.8 22.1 1.0 O A:HOH764 4.8 22.2 1.0 CB A:ASN32 4.8 12.8 1.0 N A:ASP53 4.8 12.4 1.0 N A:ASN32 4.8 17.1 1.0 C A:ASP27 4.9 15.9 1.0 CA A:ASN32 4.9 15.6 1.0 CB A:ASN29 4.9 16.1 1.0 O A:ASN32 4.9 20.5 1.0 O A:GLY52 4.9 18.3 1.0 O A:THR30 4.9 21.7 1.0

R.D.Wind, J.C.Uitdehaag, R.M.Buitelaar, B.W.Dijkstra, L.Dijkhuizen. Engineering of Cyclodextrin Product Specificity and pH Optima of the Thermostable Cyclodextrin Glycosyltransferase From Thermoanaerobacterium Thermosulfurigenes EM1. J.Biol.Chem. V. 273 5771 1998.
ISSN: ISSN 0021-9258
PubMed: 9488711
DOI: 10.1074/JBC.273.10.5771