Calcium in PDB 3wms: The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans

All present enzymatic activity of The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans:
2.4.1.19;

The structure of The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans, PDB code: 3wms was solved by T.Xie, Y.J.Hou, D.F.Li, Y.Yue, S.J.Qian, Y.P.Chao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.64 / 2.30
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	102.589, 102.589, 114.371, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / 22.1

The binding sites of Calcium atom in the The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans (pdb code 3wms). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans, PDB code: 3wms:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca801 b:26.0 occ:1.00 OD1 A:ASN170 2.4 22.3 1.0 O A:HOH905 2.4 22.8 1.0 O A:HIS264 2.4 20.3 1.0 O A:HOH907 2.4 20.4 1.0 O A:HOH902 2.4 23.8 1.0 OD1 A:ASP230 2.4 24.6 1.0 O A:ILE221 2.5 22.9 1.0 OD2 A:ASP230 2.5 27.5 1.0 CG A:ASP230 2.8 26.6 1.0 CG A:ASN170 3.5 28.4 1.0 C A:ILE221 3.6 25.2 1.0 C A:HIS264 3.7 24.0 1.0 ND2 A:ASN170 4.0 23.3 1.0 CA A:ILE221 4.2 23.2 1.0 O A:ASN170 4.3 24.0 1.0 CB A:ASP230 4.3 24.7 1.0 O A:LYS223 4.4 27.1 1.0 CB A:HIS264 4.5 25.3 1.0 CG A:MET265 4.5 24.6 1.0 O A:GLY220 4.5 27.2 1.0 N A:MET265 4.5 22.8 1.0 CA A:MET265 4.5 23.3 1.0 O A:HOH944 4.5 25.7 1.0 CA A:HIS264 4.6 24.3 1.0 CB A:ASN170 4.7 23.3 1.0 N A:TYR222 4.7 24.6 1.0 ND1 A:HIS207 4.8 24.3 1.0 CG2 A:ILE221 4.8 19.1 1.0 O A:ILE231 4.8 25.2 1.0 CA A:TYR222 5.0 27.4 1.0 CA A:ASN170 5.0 29.0 1.0

Calcium binding site 2 out of 2 in the The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Crystal Structure of Y195I Mutant Alpha-Cyclodextrin Glycosyltransferase From Paenibacillus Macerans within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca802 b:35.9 occ:1.00 OD1 A:ASN64 2.3 41.6 1.0 OD2 A:ASP84 2.4 34.5 1.0 O A:GLY82 2.4 33.5 1.0 O A:HOH1150 2.4 30.0 1.0 OD1 A:ASN63 2.5 27.9 1.0 O A:ASP60 2.5 37.1 1.0 OD1 A:ASP58 2.5 37.4 1.0 CG A:ASP58 3.3 38.2 1.0 CG A:ASP84 3.4 34.8 1.0 CG A:ASN64 3.4 42.0 1.0 C A:GLY82 3.4 34.1 1.0 C A:ASP60 3.4 37.7 1.0 CG A:ASN63 3.6 31.7 1.0 OD2 A:ASP58 3.7 35.8 1.0 CB A:ASP84 3.8 34.5 1.0 CA A:GLY82 3.9 33.2 1.0 N A:ASN64 4.1 37.1 1.0 O A:ALA142 4.1 34.3 1.0 ND2 A:ASN64 4.1 43.6 1.0 N A:ASP60 4.2 40.2 1.0 ND2 A:ASN63 4.2 34.2 1.0 N A:ARG61 4.2 35.8 1.0 CA A:ARG61 4.3 40.7 1.0 CA A:ASP60 4.3 38.1 1.0 CA A:ASN64 4.4 36.0 1.0 CB A:ASP58 4.4 34.9 1.0 OD1 A:ASP84 4.4 33.0 1.0 C A:ASN63 4.5 34.1 1.0 CB A:ASN64 4.5 35.0 1.0 CA A:ASP58 4.6 32.2 1.0 N A:GLY83 4.6 30.7 1.0 N A:ASP84 4.6 29.2 1.0 C A:GLY83 4.7 30.7 1.0 CB A:ASP60 4.7 41.3 1.0 C A:ARG61 4.8 41.4 1.0 O A:HOH926 4.8 28.9 1.0 N A:ASN63 4.8 38.0 1.0 CB A:ASN63 4.8 29.7 1.0 CA A:ASP84 4.9 30.6 1.0 O A:ASN63 4.9 41.4 1.0 N A:GLY59 4.9 35.9 1.0 O A:GLY83 4.9 29.6 1.0 CA A:ASN63 4.9 38.0 1.0 CA A:GLY83 5.0 30.1 1.0 C A:ASP58 5.0 35.2 1.0

T.Xie, Y.J.Hou, D.F.Li, Y.Yue, S.J.Qian, Y.P.Chao. Structural Basis of A Mutant Y195I Alpha-Cyclodextrin Glycosyltransferase with Switched Product Specificity From Alpha-Cyclodextrin to Beta-/ Gamma-Cyclodextrin J.Biotechnol. V.-183 92 2014.
ISSN: ISSN 0168-1656
PubMed: 24637377
DOI: 10.1016/J.JBIOTEC.2014.03.014