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3H53

Crystal Structure of human 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
A0016052biological_processcarbohydrate catabolic process
A0016139biological_processglycoside catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019377biological_processglycolipid catabolic process
A0042803molecular_functionprotein homodimerization activity
A0070062cellular_componentextracellular exosome
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004557molecular_functionalpha-galactosidase activity
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005975biological_processcarbohydrate metabolic process
B0006629biological_processlipid metabolic process
B0008456molecular_functionalpha-N-acetylgalactosaminidase activity
B0009311biological_processoligosaccharide metabolic process
B0016020cellular_componentmembrane
B0016052biological_processcarbohydrate catabolic process
B0016139biological_processglycoside catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0019377biological_processglycolipid catabolic process
B0042803molecular_functionprotein homodimerization activity
B0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00512
Number of Residues16
DetailsALPHA_GALACTOSIDASE Alpha-galactosidase signature. GYtyLnIDDc.Wigg....RD
ChainResidueDetails
AGLY71-ASP86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17693683","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19683538","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19683538","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uas
ChainResidueDetails
AASP156
AASP217

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uas
ChainResidueDetails
BASP156
BASP217

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PDB entries from 2025-12-03

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