4J5T
Crystal structure of Processing alpha-Glucosidase I
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000324 | cellular_component | fungal-type vacuole |
A | 0004573 | molecular_function | Glc3Man9GlcNAc2 oligosaccharide glucosidase activity |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006487 | biological_process | protein N-linked glycosylation |
A | 0006491 | biological_process | N-glycan processing |
A | 0009272 | biological_process | fungal-type cell wall biogenesis |
A | 0009311 | biological_process | oligosaccharide metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0070880 | biological_process | fungal-type cell wall beta-glucan biosynthetic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23536181","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23536181","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23536181","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |