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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
A0008152biological_processmetabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102483molecular_functionscopolin beta-glucosidase activity
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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8L7J2
ChainResidueDetails
AGLU191

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055
ChainResidueDetails
AGLU407

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIR, ECO:0007744|PDB:3AIS
ChainResidueDetails
AGLN43
AGLU462

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2
ChainResidueDetails
AHIS145
ATYR334

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIR
ChainResidueDetails
AASN190

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9
ChainResidueDetails
AGLU407

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIS
ChainResidueDetails
ATRP455
APHE471

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건을2024-04-17부터공개중

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