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1CBG

THE CRYSTAL STRUCTURE OF A CYANOGENIC BETA-GLUCOSIDASE FROM WHITE CLOVER (TRIFOLIUM REPENS L.), A FAMILY 1 GLYCOSYL-HYDROLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102483molecular_functionscopolin beta-glucosidase activity
Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGRN
ChainResidueDetails
AILE393-ASN401

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FvFGtAsSAFQyEgA
ChainResidueDetails
APHE23-ALA37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q7XSK0
ChainResidueDetails
AGLU183

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q7XSK0
ChainResidueDetails
AGLU397

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2
ChainResidueDetails
AGLN33
AHIS137
ATYR326

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8GU20
ChainResidueDetails
AASN182

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9
ChainResidueDetails
AGLU397

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN209
AASN401

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 442
ChainResidueDetails
AARG91modifies pKa
AHIS137transition state stabiliser
AGLU183proton shuttle (general acid/base)
AASN324modifies pKa, steric role
ATYR326modifies pKa
AGLU397covalent catalysis

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PDB entries from 2024-04-24

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