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1KTC

The Structure of alpha-N-Acetylgalactosaminidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004557molecular_functionalpha-galactosidase activity
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005975biological_processcarbohydrate metabolic process
A0006629biological_processlipid metabolic process
A0008456molecular_functionalpha-N-acetylgalactosaminidase activity
A0009311biological_processoligosaccharide metabolic process
A0016020cellular_componentmembrane
A0016139biological_processglycoside catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019377biological_processglycolipid catabolic process
Functional Information from PROSITE/UniProt
site_idPS00512
Number of Residues17
DetailsALPHA_GALACTOSIDASE Alpha-galactosidase signature. GYkyInIDDc.Waakq...RD
ChainResidueDetails
AGLY54-ASP70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12005440","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uas
ChainResidueDetails
AASP201
AASP140

243911

PDB entries from 2025-10-29

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