7P4C
Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with noncovalent Cyclophellitol Sulfamidate probe KK131
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0003824 | molecular_function | catalytic activity |
| AAA | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| AAA | 0005975 | biological_process | carbohydrate metabolic process |
| AAA | 0016740 | molecular_function | transferase activity |
| AAA | 0016757 | molecular_function | glycosyltransferase activity |
| AAA | 0030246 | molecular_function | carbohydrate binding |
| AAA | 0033825 | molecular_function | oligosaccharide 4-alpha-D-glucosyltransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23132856","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P31434","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P31434","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23132856","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
