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 | 6 |
| Details | ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:Q06GJ0, ECO:0000305|PubMed:29239122, ECO:0007744|PDB:5OAR |
| Chain | Residue | Details |
| B | ASP222 | |
| B | HIS275 | |
| B | GLU346 | |
| D | ASP222 | |
| D | HIS275 | |
| D | GLU346 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Important determinant of glycosidic bond specificity => ECO:0000250|UniProtKB:Q06GJ0 |
| Chain | Residue | Details |
| B | VAL306 | |
| D | VAL306 | |
| C | SER83 | |
| C | SER84 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Essential for chitooligosaccharide substrate binding => ECO:0000250|UniProtKB:Q06GJ0 |
| Chain | Residue | Details |
| B | GLU307 | |
| B | TRP482 | |
| D | GLU307 | |
| D | TRP482 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:29239122 |
| Chain | Residue | Details |
| B | ASN525 | |
| D | ASN525 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (HexNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:29239122 |
| Chain | Residue | Details |
| B | ASN318 | |
| B | ASN387 | |
| D | ASN318 | |
| D | ASN387 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:29239122, ECO:0007744|PDB:5OAR |
| Chain | Residue | Details |
| B | ASN353 | |
| D | ASN353 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:17509134, ECO:0000269|PubMed:29239122, ECO:0007744|PDB:5OAR |
| Chain | Residue | Details |
| B | ASN428 | |
| B | ASN500 | |
| D | ASN428 | |
| D | ASN500 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| B | ASN525 | |
| D | ASN525 |
