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2JF7

Structure of Strictosidine Glucosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009820biological_processalkaloid metabolic process
A0009821biological_processalkaloid biosynthetic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0050422molecular_functionstrictosidine beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0009820biological_processalkaloid metabolic process
B0009821biological_processalkaloid biosynthetic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0050422molecular_functionstrictosidine beta-glucosidase activity
Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGaGgSAYQcEgA
ChainResidueDetails
APHE47-ALA61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q7XSK0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PDB","id":"3ZJ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17890378","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZJ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17890378","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JF6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8L7J2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9SPP9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Controls the gate shape and acceptance of substrates"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU207
AGLU416
AASN343

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU207
BGLU416
BASN343

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU207
AGLU416

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU207
BGLU416

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU207
ATYR345
AGLU416
AASN343
ATHR210
AARG115

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU207
BTYR345
BGLU416
BASN343
BTHR210
BARG115

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PDB entries from 2025-12-10

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