Calcium in PDB 3bmv: Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P

All present enzymatic activity of Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P:
2.4.1.19;

The structure of Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P, PDB code: 3bmv was solved by H.J.Rozeboom, N.Van Oosterwijk, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.83 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.625, 96.016, 114.159, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 16.3

The binding sites of Calcium atom in the Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P (pdb code 3bmv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P, PDB code: 3bmv:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca684 b:9.2 occ:1.00 O A:HIS234 2.4 5.4 1.0 OD1 A:ASN140 2.4 5.5 1.0 O A:HOH810 2.5 9.2 1.0 OD2 A:ASP200 2.5 6.1 1.0 O A:ILE191 2.5 4.8 1.0 O A:HOH699 2.5 8.8 1.0 O A:HOH729 2.5 8.9 1.0 OD1 A:ASP200 2.6 5.2 1.0 CG A:ASP200 2.9 5.6 1.0 CG A:ASN140 3.5 6.3 1.0 C A:ILE191 3.6 5.2 1.0 C A:HIS234 3.6 6.0 1.0 ND2 A:ASN140 4.0 6.7 1.0 CA A:ILE191 4.2 4.7 1.0 O A:ASN140 4.3 6.5 1.0 CB A:ASP200 4.4 5.2 1.0 CG A:MET235 4.4 5.5 1.0 O A:ARG193 4.5 6.5 1.0 N A:MET235 4.5 5.8 1.0 CB A:HIS234 4.5 6.0 1.0 CA A:MET235 4.5 5.6 1.0 O A:GLY190 4.6 5.1 1.0 ND1 A:HIS177 4.6 6.6 1.0 CA A:HIS234 4.6 5.9 1.0 N A:TYR192 4.7 5.1 1.0 CE1 A:HIS177 4.7 7.2 1.0 CB A:ASN140 4.7 6.5 1.0 O A:LEU201 4.8 5.8 1.0 O A:HOH1316 4.8 12.3 1.0 CG2 A:ILE191 4.8 4.5 1.0 NE2 A:GLN203 4.9 6.2 1.0 OE1 A:GLN203 4.9 6.4 1.0 CA A:TYR192 5.0 5.8 1.0

Calcium binding site 2 out of 2 in the Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Cyclodextrin Glycosyl Transferase From Thermoanerobacterium Thermosulfurigenes EM1 Mutant S77P within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca685 b:11.4 occ:1.00 OD1 A:ASN33 2.3 7.2 1.0 OD1 A:ASN32 2.4 6.4 1.0 OD2 A:ASP53 2.4 7.1 1.0 O A:GLY51 2.4 5.3 1.0 OD1 A:ASP27 2.4 8.1 1.0 O A:ASN29 2.5 6.6 1.0 O A:HOH807 2.5 12.1 1.0 CG A:ASP27 3.4 7.5 1.0 CG A:ASP53 3.4 5.6 1.0 CG A:ASN32 3.5 7.3 1.0 CG A:ASN33 3.5 7.7 1.0 C A:GLY51 3.5 5.2 1.0 C A:ASN29 3.5 7.4 1.0 CB A:ASP53 3.9 5.0 1.0 CA A:GLY51 4.0 5.2 1.0 ND2 A:ASN32 4.0 8.0 1.0 OD2 A:ASP27 4.0 8.7 1.0 N A:ASN33 4.1 6.9 1.0 N A:ASN29 4.2 7.5 1.0 ND2 A:ASN33 4.3 7.2 1.0 O A:TYR112 4.3 7.5 1.0 CA A:ASN33 4.4 7.3 1.0 CA A:ASN29 4.4 7.8 1.0 N A:THR30 4.4 7.2 1.0 CB A:ASP27 4.4 6.7 1.0 C A:ASN32 4.4 6.9 1.0 CA A:THR30 4.4 7.4 1.0 CA A:ASP27 4.4 6.7 1.0 OD1 A:ASP53 4.4 5.7 1.0 CB A:ASN33 4.5 7.1 1.0 N A:GLY52 4.7 5.3 1.0 CB A:ASN32 4.7 6.4 1.0 C A:GLY52 4.8 5.0 1.0 C A:ASP27 4.8 6.7 1.0 O A:HOH730 4.8 10.6 1.0 C A:THR30 4.8 7.1 1.0 N A:GLY28 4.9 6.7 1.0 N A:ASP53 4.9 5.0 1.0 CA A:ASN32 4.9 6.6 1.0 N A:ASN32 4.9 6.5 1.0 CB A:ASN29 4.9 8.5 1.0 O A:ASN32 4.9 6.9 1.0 O A:GLY52 5.0 5.2 1.0 O A:THR30 5.0 6.9 1.0

R.M.Kelly, H.Leemhuis, H.J.Rozeboom, N.Van Oosterwijk, B.W.Dijkstra, L.Dijkhuizen. Elimination of Competing Hydrolysis and Coupling Side Reactions of A Cyclodextrin Glucanotransferase By Directed Evolution. Biochem.J. V. 413 517 2008.
ISSN: ISSN 0264-6021
PubMed: 18422488
DOI: 10.1042/BJ20080353