3OZP
Crystal Structure of insect beta-N-acetyl-D-hexosaminidase OfHex1 complexed with PUGNAc
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
A | 0005764 | cellular_component | lysosome |
A | 0005886 | cellular_component | plasma membrane |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006032 | biological_process | chitin catabolic process |
A | 0006517 | biological_process | protein deglycosylation |
A | 0006689 | biological_process | ganglioside catabolic process |
A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030203 | biological_process | glycosaminoglycan metabolic process |
A | 0102148 | molecular_function | obsolete N-acetyl-beta-D-galactosaminidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE OAN A 1 |
Chain | Residue |
A | ARG220 |
A | TRP490 |
A | TRP524 |
A | GLU526 |
A | HOH993 |
A | HIS303 |
A | VAL327 |
A | GLU328 |
A | ASP367 |
A | GLU368 |
A | TRP448 |
A | TYR475 |
A | ASP477 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:21106526 |
Chain | Residue | Details |
A | ASP249 | |
A | HIS303 | |
A | GLU368 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Important determinant of glycosidic bond specificity => ECO:0000269|PubMed:23300622 |
Chain | Residue | Details |
A | VAL327 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Essential for chitooligosaccharide substrate binding => ECO:0000269|PubMed:23300622 |
Chain | Residue | Details |
A | GLU328 | |
A | TRP490 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25155420, ECO:0000269|PubMed:30135205, ECO:0007744|PDB:3WMB, ECO:0007744|PDB:3WMC, ECO:0007744|PDB:5Y0V, ECO:0007744|PDB:5Y1B |
Chain | Residue | Details |
A | ASN164 | |
A | ASN375 |