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 | ACT_SITE: Proton donor => ECO:0000269|PubMed:11329289 |
Chain | Residue | Details |
A | GLU355 | |
B | GLU355 | |
C | GLU355 | |
D | GLU355 | |
E | GLU355 | |
F | GLU355 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | SITE: Not glycosylated => ECO:0000269|PubMed:11447134 |
Chain | Residue | Details |
A | ASN497 | |
B | ASN497 | |
C | ASN497 | |
D | ASN497 | |
E | ASN497 | |
F | ASN497 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11447134, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN84 | |
B | ASN84 | |
C | ASN84 | |
D | ASN84 | |
E | ASN84 | |
F | ASN84 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11447134 |
Chain | Residue | Details |
A | ASN142 | |
E | ASN190 | |
F | ASN142 | |
F | ASN190 | |
A | ASN190 | |
B | ASN142 | |
B | ASN190 | |
C | ASN142 | |
C | ASN190 | |
D | ASN142 | |
D | ASN190 | |
E | ASN142 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11447134, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN327 | |
B | ASN327 | |
C | ASN327 | |
D | ASN327 | |
E | ASN327 | |
F | ASN327 |
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 |