3ZJ7
Crystal structure of strictosidine glucosidase in complex with inhibitor-1
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 | 0009820 | biological_process | alkaloid metabolic process |
| A | 0009821 | biological_process | alkaloid biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0050422 | molecular_function | strictosidine beta-glucosidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0009820 | biological_process | alkaloid metabolic process |
| B | 0009821 | biological_process | alkaloid biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0050422 | molecular_function | strictosidine beta-glucosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C1K A 1509 |
| Chain | Residue |
| A | GLN57 |
| A | TRP473 |
| A | TYR481 |
| A | HIS161 |
| A | ASN206 |
| A | GLU207 |
| A | THR210 |
| A | TYR345 |
| A | GLU416 |
| A | TRP465 |
| A | GLU472 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C1K B 1509 |
| Chain | Residue |
| B | GLN57 |
| B | HIS161 |
| B | ASN206 |
| B | GLU207 |
| B | THR210 |
| B | TYR345 |
| B | GLU416 |
| B | TRP465 |
| B | GLU472 |
| B | TRP473 |
| B | TYR481 |
Functional Information from PROSITE/UniProt
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FiFGaGgSAYQcEgA |
| Chain | Residue | Details |
| A | PHE47-ALA61 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q7XSK0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PDB","id":"3ZJ8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17890378","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZJ8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17890378","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JF6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8L7J2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9SPP9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Controls the gate shape and acceptance of substrates"} |
| Chain | Residue | Details |
