Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4IIF

Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009251biological_processglucan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
A0102483molecular_functionscopolin beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009251biological_processglucan catabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
B0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. LLKaElgfqGFVMSDwgA
ChainResidueDetails
ALEU266-ALA283

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP280
BASP280

site_idSWS_FT_FI2
Number of Residues30
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN61
AASN542
AASN564
AASN658
AASN668
AASN690
AASN712
BASN61
BASN211
BASN252
BASN315
AASN211
BASN322
BASN354
BASN387
BASN442
BASN523
BASN542
BASN564
BASN658
BASN668
BASN690
AASN252
BASN712
AASN315
AASN322
AASN354
AASN387
AASN442
AASN523

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon