6C9Z
THE CRYSTAL STRUCTURE OF THE alpha-Glucosidase (GH 31) W169Y mutant FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with voglibose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030246 | molecular_function | carbohydrate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0030246 | molecular_function | carbohydrate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue VOG A 701 |
Chain | Residue |
A | ASP73 |
A | ASP420 |
A | HIS478 |
A | HOH811 |
A | HOH827 |
A | TYR169 |
A | ASP197 |
A | ILE198 |
A | TRP271 |
A | TRP305 |
A | ASP307 |
A | ARG404 |
A | TRP417 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue VOG B 701 |
Chain | Residue |
B | ASP73 |
B | TYR169 |
B | ASP197 |
B | ILE198 |
B | TRP271 |
B | TRP305 |
B | ASP307 |
B | ARG404 |
B | TRP417 |
B | ASP420 |
B | PHE453 |
B | HIS478 |
B | HOH804 |
B | HOH809 |
B | HOH816 |
Functional Information from PROSITE/UniProt
site_id | PS00129 |
Number of Residues | 8 |
Details | GLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GFWnDMNE |
Chain | Residue | Details |
A | GLY303-GLU310 |