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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 0016787 | molecular_function | hydrolase activity |
| 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 |
