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8IBT

Crystal structure of GH42 beta-galactosidase BiBga42A from Bifidobacterium longum subspecies infantis E318S mutant in complex with lacto-N-tetraose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004565molecular_functionbeta-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0009341cellular_componentbeta-galactosidase complex
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004565molecular_functionbeta-galactosidase activity
B0005975biological_processcarbohydrate metabolic process
B0009341cellular_componentbeta-galactosidase complex
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O69315
ChainResidueDetails
AGLU160
BGLU160

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O69315
ChainResidueDetails
ASER318
BSER318

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O69315
ChainResidueDetails
AARG121
AASN159
ATRP326
AGLU366
BARG121
BASN159
BTRP326
BGLU366

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PDB entries from 2024-11-06

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