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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE G3I A 316 |
| Chain | Residue |
| A | GLU43 |
| A | HIS205 |
| A | GLU233 |
| A | TRP273 |
| A | TRP281 |
| A | HOH544 |
| A | HOH548 |
| A | HOH554 |
| A | HOH651 |
| A | HOH751 |
| A | ASN44 |
| A | LYS47 |
| A | HIS80 |
| A | TRP84 |
| A | GLN87 |
| A | ASN126 |
| A | GLU127 |
| A | GLN203 |
Functional Information from PROSITE/UniProt
| site_id | PS00591 |
| Number of Residues | 11 |
| Details | GH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVDVrITELDI |
| Chain | Residue | Details |
| A | GLY226-ILE236 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 310 |
| Details | Domain: {"description":"GH10","evidences":[{"source":"PROSITE-ProRule","id":"PRU01096","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"7918478","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| A | GLU127 | |
| A | GLU233 | |
| A | ASP235 | |
| A | HIS205 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1exp |
| Chain | Residue | Details |
| A | GLU127 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 548 |
| Chain | Residue | Details |
| A | GLU127 | proton acceptor, proton donor |
| A | ASN169 | electrostatic stabiliser |
| A | HIS205 | electrostatic stabiliser |
| A | GLU233 | electrostatic stabiliser, nucleofuge, nucleophile |
| A | ASP235 | electrostatic stabiliser |
