Calcium in PDB 2vno: Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand.

The structure of Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand., PDB code: 2vno was solved by K.J.Gregg, R.Finn, D.W.Abbott, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.45
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.691, 98.551, 49.128, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22.6

The binding sites of Calcium atom in the Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand. (pdb code 2vno). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand., PDB code: 2vno:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1213 b:13.6 occ:1.00 O A:LYS137 2.3 12.7 1.0 O A:LYS190 2.3 13.9 1.0 OD2 A:ASP194 2.4 14.1 1.0 O A:HOH2264 2.4 15.3 1.0 O A:ALA187 2.4 15.1 1.0 O A:HOH2181 2.4 14.0 1.0 OD1 A:ASP194 2.7 13.3 1.0 CG A:ASP194 2.9 13.2 1.0 C A:ALA187 3.4 14.9 1.0 C A:LYS137 3.4 12.9 1.0 C A:LYS190 3.5 13.6 1.0 CA A:ALA187 3.9 13.6 1.0 CB A:ALA187 4.0 13.3 1.0 N A:LYS137 4.1 11.8 1.0 CA A:LYS137 4.1 12.7 1.0 CB A:LYS137 4.2 14.1 1.0 N A:LYS190 4.2 15.5 1.0 CA A:THR191 4.3 12.5 1.0 N A:THR191 4.4 12.3 1.0 CB A:ASP194 4.4 10.6 1.0 CA A:LYS190 4.4 15.3 1.0 N A:VAL138 4.5 12.1 1.0 O A:HOH2269 4.5 22.9 1.0 C A:THR191 4.5 12.1 1.0 N A:GLY188 4.6 16.2 1.0 O A:HOH2182 4.6 20.1 1.0 O A:TRP192 4.7 14.0 1.0 CA A:VAL138 4.7 12.4 1.0 N A:TRP192 4.8 13.7 1.0 O A:GLN134 4.8 18.3 1.0 N A:GLU189 4.9 17.8 1.0 C A:GLY188 4.9 17.0 1.0 CA A:GLY188 4.9 16.5 1.0 CB A:LYS190 4.9 17.8 1.0

Calcium binding site 2 out of 2 in the Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Family 51 Carbohydrate Binding Module From A Family 98 Glycoside Hydrolase Produced By Clostridium Perfringens in Complex with Blood Group B-Trisaccharide Ligand. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1214 b:13.4 occ:1.00 O B:LYS190 2.3 14.2 1.0 O B:LYS137 2.3 15.1 1.0 O B:ALA187 2.3 13.3 1.0 OD2 B:ASP194 2.4 16.1 1.0 O B:HOH2260 2.4 15.9 1.0 O B:HOH2184 2.5 13.9 1.0 OD1 B:ASP194 2.8 13.5 1.0 CG B:ASP194 2.9 13.9 1.0 C B:ALA187 3.4 14.1 1.0 C B:LYS137 3.4 13.9 1.0 C B:LYS190 3.5 13.8 1.0 CA B:ALA187 3.9 12.8 1.0 CB B:ALA187 4.1 13.8 1.0 N B:LYS137 4.1 13.7 1.0 CA B:LYS137 4.2 13.2 1.0 CB B:LYS137 4.2 14.8 1.0 N B:LYS190 4.2 16.1 1.0 CA B:THR191 4.3 13.3 1.0 N B:THR191 4.4 12.5 1.0 CA B:LYS190 4.4 16.2 1.0 CB B:ASP194 4.4 10.9 1.0 N B:VAL138 4.5 13.1 1.0 C B:THR191 4.5 12.9 1.0 O B:HOH2183 4.6 21.6 1.0 N B:GLY188 4.6 15.2 1.0 O B:HOH2187 4.6 28.7 1.0 CA B:VAL138 4.7 13.6 1.0 N B:TRP192 4.8 13.8 1.0 O B:TRP192 4.8 13.3 1.0 N B:GLU189 4.8 17.9 1.0 O B:GLN134 4.8 16.8 1.0 CA B:GLY188 4.9 15.8 1.0 C B:GLY188 4.9 17.8 1.0

K.J.Gregg, R.Finn, D.W.Abbott, A.B.Boraston. Divergent Modes of Glycan Recognition By A New Family of Carbohydrate-Binding Modules J.Biol.Chem. V. 283 12604 2008.
ISSN: ISSN 0021-9258
PubMed: 18292090
DOI: 10.1074/JBC.M709865200