3PTK
The crystal structure of rice (Oryza sativa L.) Os4BGlu12
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 | 0016787 | molecular_function | hydrolase 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 |
| 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 | 0016787 | molecular_function | hydrolase 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS A 1164 |
| Chain | Residue |
| A | GLN29 |
| A | HOH611 |
| A | GLU179 |
| A | TYR322 |
| A | TRP365 |
| A | GLU393 |
| A | TRP442 |
| A | GLU449 |
| A | TRP450 |
| A | PHE458 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 487 |
| Chain | Residue |
| A | ASP66 |
| A | HIS69 |
| B | GLU36 |
| B | HIS69 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TRS B 1165 |
| Chain | Residue |
| B | GLN29 |
| B | HIS133 |
| B | GLU179 |
| B | TYR322 |
| B | TRP365 |
| B | GLU393 |
| B | TRP442 |
| B | GLU449 |
| B | TRP450 |
| B | PHE458 |
| B | HOH562 |
| B | HOH564 |
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 | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q7XKV4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q7XKV4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q7XSK0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9SPP9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q1XH05","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
