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1XC6

Native Structure Of Beta-Galactosidase from Penicillium sp. in complex with Galactose

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004565molecular_functionbeta-galactosidase activity
A0005534molecular_functiongalactose binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005773cellular_componentvacuole
A0005975biological_processcarbohydrate metabolic process
A0005990biological_processlactose catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PROSITE/UniProt
site_idPS01182
Number of Residues13
DetailsGLYCOSYL_HYDROL_F35 Glycosyl hydrolases family 35 putative active site. GGPIIlyQpENEY
ChainResidueDetails
AGLY189-TYR201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AGLU200

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255
ChainResidueDetails
AGLU299

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15491613, ECO:0007744|PDB:1XC6
ChainResidueDetails
ATYR96
AASN140
AASN199
ATYR365

site_idSWS_FT_FI4
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15491613, ECO:0007744|PDB:1XC6
ChainResidueDetails
AASN374
AASN456
AASN625
AASN707
AASN763
AASN780
AASN917

219140

PDB entries from 2024-05-01

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