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3WQ4

Crystal structure of beta-primeverosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0050535molecular_functionbeta-primeverosidase activity
A0102402molecular_function2-phenylethyl 6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside glucosidase (Yabukita) activity
A0102404molecular_functionlinalyl 6-O-alpha-L-arabinopyranosyl-beta-D-glucopyranoside glucosidase (Yabukita) activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0050535molecular_functionbeta-primeverosidase activity
B0102402molecular_function2-phenylethyl 6-O-beta-D-xylopyranosyl-beta-D-glucopyranoside glucosidase (Yabukita) activity
B0102404molecular_functionlinalyl 6-O-alpha-L-arabinopyranosyl-beta-D-glucopyranoside glucosidase (Yabukita) activity
Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IYITENGMG
ChainResidueDetails
AILE412-GLY420

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FvFGaAsSAYQfEgA
ChainResidueDetails
APHE43-ALA57

219869

PDB entries from 2024-05-15

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