3PTM
The crystal structure of rice (Oryza sativa L.) Os4BGlu12 with 2-fluoroglucopyranoside
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004338 | molecular_function | glucan exo-1,3-beta-glucosidase activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004565 | molecular_function | beta-galactosidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0033907 | molecular_function | beta-D-fucosidase activity |
| A | 0047701 | molecular_function | beta-L-arabinosidase activity |
| A | 0080083 | molecular_function | beta-gentiobiose beta-glucosidase activity |
| A | 0102483 | molecular_function | scopolin beta-glucosidase activity |
| B | 0004338 | molecular_function | glucan exo-1,3-beta-glucosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004565 | molecular_function | beta-galactosidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0033907 | molecular_function | beta-D-fucosidase activity |
| B | 0047701 | molecular_function | beta-L-arabinosidase activity |
| B | 0080083 | molecular_function | beta-gentiobiose beta-glucosidase activity |
| B | 0102483 | molecular_function | scopolin beta-glucosidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGtAsSSYQyEgG |
| Chain | Residue | Details |
| A | PHE19-GLY33 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q7XKV4 |
| Chain | Residue | Details |
| A | GLU179 | |
| B | GLU179 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q7XKV4 |
| Chain | Residue | Details |
| A | GLU393 | |
| B | GLU393 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q7XSK0 |
| Chain | Residue | Details |
| A | GLN29 | |
| B | TYR322 | |
| B | TRP442 | |
| B | GLU449 | |
| A | HIS133 | |
| A | ASN178 | |
| A | TYR322 | |
| A | TRP442 | |
| A | GLU449 | |
| B | GLN29 | |
| B | HIS133 | |
| B | ASN178 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9 |
| Chain | Residue | Details |
| A | GLU393 | |
| B | GLU393 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q1XH05 |
| Chain | Residue | Details |
| A | PHE458 | |
| B | PHE458 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | ASN98 | |
| B | ASN401 | |
| A | ASN205 | |
| A | ASN337 | |
| A | ASN347 | |
| A | ASN401 | |
| B | ASN98 | |
| B | ASN205 | |
| B | ASN337 | |
| B | ASN347 |
