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2DGA

Crystal structure of hexameric beta-glucosidase in wheat

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009507cellular_componentchloroplast
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102726molecular_functionDIMBOA glucoside beta-D-glucosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1001
ChainResidue
AGLN270
AASP271
ASER366
AARG434
AHOH1465
AHOH1472
AHOH1589
AHOH1820

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1314
ChainResidue
AASP262
AASN332
ATYR334
ATRP379
AGOL1315
AHOH1741
AGLU191

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 1315
ChainResidue
AGLN43
AGLU191
ATYR334
ATRP379
AGLU407
ATRP455
AGLU462
ATRP463
APHE471
AGOL1314
AHOH1415

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1316
ChainResidue
AHIS205
AGLU462
ATRP463
ASER464
AHOH1449

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VFITENGIA
ChainResidueDetails
AVAL403-ALA411

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlFGaStSAYQiEgA
ChainResidueDetails
APHE33-ALA47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q8L7J2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10055","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21421370","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3AIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AIS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8L7J2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21421370","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3AIR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9SPP9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21421370","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3AIS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU407
AGLU191
AASN332

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
AGLU407
AGLU191

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1cbg
ChainResidueDetails
ATYR334
AGLU407
AARG101
AASN332
AGLU191
ATHR194

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PDB entries from 2025-12-24

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