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4IUG

Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS01182
Number of Residues13
DetailsGLYCOSYL_HYDROL_F35 Glycosyl hydrolases family 35 putative active site. GGPVIlyQpENEY
ChainResidueDetails
AGLY189-TYR201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23688418","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23688418","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23688418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IUG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23688418","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IUG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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