5OAR
Crystal structure of native beta-N-acetylhexosaminidase isolated from Aspergillus oryzae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OAR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OAR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"Q06GJ0","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5OAR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important determinant of glycosidic bond specificity","evidences":[{"source":"UniProtKB","id":"Q06GJ0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Essential for chitooligosaccharide substrate binding","evidences":[{"source":"UniProtKB","id":"Q06GJ0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (HexNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OAR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17509134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29239122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OAR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
