3AIR
Crystal structure of beta-glucosidase in wheat complexed with 2-deoxy-2-fluoroglucoside and dinitrophenol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008422 | molecular_function | beta-glucosidase activity |
A | 0009507 | cellular_component | chloroplast |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0102483 | molecular_function | scopolin beta-glucosidase activity |
A | 0102726 | molecular_function | DIMBOA glucoside beta-D-glucosidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00572 |
Number of Residues | 9 |
Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. VFITENGIA |
Chain | Residue | Details |
A | VAL403-ALA411 |
site_id | PS00653 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlFGaStSAYQiEgA |
Chain | Residue | Details |
A | PHE33-ALA47 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8L7J2 |
Chain | Residue | Details |
A | GLU191 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10055 |
Chain | Residue | Details |
A | GLU407 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIR, ECO:0007744|PDB:3AIS |
Chain | Residue | Details |
A | GLN43 | |
A | GLU462 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2 |
Chain | Residue | Details |
A | HIS145 | |
A | TYR334 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIR |
Chain | Residue | Details |
A | ASN190 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9 |
Chain | Residue | Details |
A | GLU407 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21421370, ECO:0007744|PDB:3AIS |
Chain | Residue | Details |
A | TRP455 | |
A | PHE471 |