7KBJ
Co-crystal structure of alpha glucosidase with compound 9
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0005975 | biological_process | carbohydrate metabolic process |
| H | 0030246 | molecular_function | carbohydrate binding |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0005975 | biological_process | carbohydrate metabolic process |
| J | 0030246 | molecular_function | carbohydrate binding |
Functional Information from PROSITE/UniProt
| site_id | PS00129 |
| Number of Residues | 8 |
| Details | GLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. YVWnDMNE |
| Chain | Residue | Details |
| A | TYR560-GLU567 |
| site_id | PS00707 |
| Number of Residues | 31 |
| Details | GLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADVGGFfknPepeLLvRWyqMGAYqPFfRA |
| Chain | Residue | Details |
| A | GLY667-ALA697 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5HJO |
| Chain | Residue | Details |
| D | ASP49 | |
| D | ASP53 | |
| B | ASP49 | |
| B | ASP53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O, ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR, ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE, ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG |
| Chain | Residue | Details |
| B | ASP98 | |
| B | ASP104 | |
| B | GLU105 | |
| D | GLN50 | |
| D | TYR55 | |
| D | ASP57 | |
| D | ASP63 | |
| D | GLU64 | |
| D | ARG91 | |
| D | ASP94 | |
| D | VAL96 | |
| D | ASP98 | |
| D | ASP104 | |
| D | GLU105 | |
| B | ASP57 | |
| B | ASP63 | |
| B | GLU64 | |
| B | ARG91 | |
| B | ASP94 | |
| B | VAL96 | |
| B | GLN50 | |
| B | TYR55 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14314 |
| Chain | Residue | Details |
| C | ARG624 | |
| C | HIS698 | |
| D | SER24 | |
| A | HIS698 | |
| C | ASP451 | |
| B | SER24 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC => ECO:0000255 |
| Chain | Residue | Details |
| B | SER89 | |
| D | SER89 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN72 | |
| D | ASN72 |
