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3AIU

Crystal structure of beta-glucosidase in rye

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0009507cellular_componentchloroplast
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 520
ChainResidue
ATHR16
AGLN270
AASP271
ASER366
AARG434
AHOH549
AHOH626
AHOH708

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 814
ChainResidue
AGLU191
ATYR334
ATRP379
AGLU407
ATRP455
AGLU462
ATRP463
AHOH536
AHOH541
AHOH608
AGLN43

Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. IFITENGIA
ChainResidueDetails
AILE403-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, ECO:0000269|PubMed:21421370, ECO:0007744|PDB:3AIW
ChainResidueDetails
AGLU407

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIW
ChainResidueDetails
AHIS145
AASN190
AGLN43
AGLU462

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2
ChainResidueDetails
ATYR334
ATRP455

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9
ChainResidueDetails
AGLU407

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q1XH05
ChainResidueDetails
APHE471

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PDB entries from 2024-06-12

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