Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030203 | biological_process | glycosaminoglycan metabolic process |
A | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 605 |
Chain | Residue |
A | ARG150 |
A | ALA423 |
A | HOH680 |
A | HOH829 |
A | HOH906 |
A | HOH983 |
A | HOH1000 |
A | HOH1081 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 606 |
Chain | Residue |
A | LYS275 |
A | LEU406 |
A | SER407 |
A | TRP408 |
A | TYR271 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 607 |
Chain | Residue |
A | ARG176 |
A | ARG179 |
A | HOH775 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 608 |
Chain | Residue |
A | LYS275 |
A | LYS275 |
A | VAL276 |
A | VAL276 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE IFG A 601 |
Chain | Residue |
A | ARG162 |
A | VAL276 |
A | ASP313 |
A | GLU314 |
A | TRP344 |
A | TRP361 |
A | TYR393 |
A | ASP395 |
A | LEU406 |
A | TRP408 |
A | TRP442 |
A | GLU444 |
A | GOL602 |
A | HOH620 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 602 |
Chain | Residue |
A | LYS275 |
A | VAL276 |
A | GLY277 |
A | PHE278 |
A | GLU314 |
A | IFG601 |
A | GOL603 |
A | HOH766 |
A | HOH887 |
A | HOH979 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 603 |
Chain | Residue |
A | SER317 |
A | HIS345 |
A | GLN346 |
A | TRP361 |
A | GLU370 |
A | GOL602 |
A | HOH659 |
A | HOH789 |
A | HOH979 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 604 |
Chain | Residue |
A | ASP264 |
A | VAL266 |
A | PRO268 |
A | ARG365 |
A | ALA409 |
A | HOH643 |
A | HOH670 |
A | HOH675 |
A | HOH682 |
A | HOH1118 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | ASP47-GLY67 | |
site_id | SWS_FT_FI2 |
Number of Residues | 126 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | TYR68-GLY194 | |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | TRP195-GLY215 | |
site_id | SWS_FT_FI4 |
Number of Residues | 19 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | GLY216-ALA235 | |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | PRO88 | |
A | LEU96 | |
A | THR119 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qba |
Chain | Residue | Details |
A | ASP313 | |
A | GLU314 | |