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1WCG

Aphid myrosinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019137molecular_functionthioglucosidase activity
A0046872molecular_functionmetal ion binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0019137molecular_functionthioglucosidase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1465
ChainResidue
AGLN19
AHIS122
AASN166
AGLU167
AGLU374
ATRP416
AGLU423
ATRP424
AGOL1466

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1466
ChainResidue
AGLU167
AGLU423
APHE432
AGOL1465
AHOH2395
AHOH2774

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B1465
ChainResidue
BGLN19
BHIS122
BASN166
BGLU167
BGLU374
BTRP416
BGLU423
BTRP424
BGOL1466

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B1466
ChainResidue
BGLU167
BTYR309
BTYR346
BGLU423
BGOL1465
BHOH2368
BHOH2369
BHOH2674
BHOH2675

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B1467
ChainResidue
BARG312
BTHR332
BSER333
BVAL334
BHOH2676

Functional Information from PROSITE/UniProt
site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FmFGtStASYQiEgG
ChainResidueDetails
APHE9-GLY23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16291087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"16291087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P29736","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU374
AGLU167
AASN307

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU374
BGLU167
BASN307

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU374
AGLU167

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
BGLU374
BGLU167

239803

PDB entries from 2025-08-06

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