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4J5T

Crystal structure of Processing alpha-Glucosidase I

Functional Information from GO Data
ChainGOidnamespacecontents
A0000324cellular_componentfungal-type vacuole
A0004573molecular_functionGlc3Man9GlcNAc2 oligosaccharide glucosidase activity
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005975biological_processcarbohydrate metabolic process
A0006487biological_processprotein N-linked glycosylation
A0006491biological_processN-glycan processing
A0009272biological_processfungal-type cell wall biogenesis
A0009311biological_processoligosaccharide metabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0070880biological_processfungal-type cell wall beta-glucan biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23536181","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23536181","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23536181","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-08-06

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