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2XN2

Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with galactose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004557molecular_functionalpha-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0051289biological_processprotein homotetramerization
A1901545biological_processresponse to raffinose
Functional Information from PROSITE/UniProt
site_idPS00512
Number of Residues16
DetailsALPHA_GALACTOSIDASE Alpha-galactosidase signature. GLemFvLDDg.Wfgh....RD
ChainResidueDetails
AGLY363-ASP378

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21827767","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21827767","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21827767","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XN2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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