1O7A
Human beta-Hexosaminidase B
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 |
| 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 |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| C | 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 |
| E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| E | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| F | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| F | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11329289","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qba |
| Chain | Residue | Details |
| A | ASP354 | |
| A | GLU355 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qba |
| Chain | Residue | Details |
| B | ASP354 | |
| B | GLU355 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qba |
| Chain | Residue | Details |
| C | ASP354 | |
| C | GLU355 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qba |
| Chain | Residue | Details |
| D | ASP354 | |
| D | GLU355 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qba |
| Chain | Residue | Details |
| E | ASP354 | |
| E | GLU355 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qba |
| Chain | Residue | Details |
| F | ASP354 | |
| F | GLU355 |
