2JF6
Structure of inactive mutant of Strictosidine Glucosidase in complex with strictosidine
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 | 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 | 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 | 17 |
| Details | BINDING SITE FOR RESIDUE S55 A 1509 |
| Chain | Residue |
| A | GLN57 |
| A | TYR345 |
| A | GLY386 |
| A | TRP388 |
| A | GLU416 |
| A | TRP465 |
| A | GLU472 |
| A | TRP473 |
| A | TYR481 |
| A | HIS161 |
| A | ASN206 |
| A | GLU207 |
| A | THR210 |
| A | PHE221 |
| A | ASN273 |
| A | MET297 |
| A | ASN343 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S55 B 1509 |
| Chain | Residue |
| B | GLN57 |
| B | HIS161 |
| B | TRP162 |
| B | ASN206 |
| B | GLU207 |
| B | THR210 |
| B | PHE221 |
| B | MET297 |
| B | TYR345 |
| B | GLY386 |
| B | TRP388 |
| B | GLU416 |
| B | TRP465 |
| B | GLU472 |
| B | TRP473 |
| B | TYR481 |
| B | HOH2035 |
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 | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q7XSK0 |
| Chain | Residue | Details |
| A | GLU207 | |
| B | GLU207 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0007744|PDB:3ZJ8 |
| Chain | Residue | Details |
| A | GLU416 | |
| B | GLU416 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17890378, ECO:0007744|PDB:2JF6, ECO:0007744|PDB:3ZJ8 |
| Chain | Residue | Details |
| A | GLN57 | |
| A | ASN206 | |
| A | GLU472 | |
| B | GLN57 | |
| B | ASN206 | |
| B | GLU472 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17890378, ECO:0007744|PDB:2JF6 |
| Chain | Residue | Details |
| A | HIS161 | |
| A | TRP465 | |
| A | TYR481 | |
| B | HIS161 | |
| B | TRP465 | |
| B | TYR481 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2 |
| Chain | Residue | Details |
| A | TYR345 | |
| B | TYR345 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9SPP9 |
| Chain | Residue | Details |
| A | GLU416 | |
| B | GLU416 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Controls the gate shape and acceptance of substrates |
| Chain | Residue | Details |
| A | TRP388 | |
| B | TRP388 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU207 | |
| A | GLU416 | |
| A | ASN343 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU207 | |
| B | GLU416 | |
| B | ASN343 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU207 | |
| A | GLU416 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU207 | |
| B | GLU416 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| A | GLU207 | |
| A | TYR345 | |
| A | GLU416 | |
| A | ASN343 | |
| A | THR210 | |
| A | ARG115 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1cbg |
| Chain | Residue | Details |
| B | GLU207 | |
| B | TYR345 | |
| B | GLU416 | |
| B | ASN343 | |
| B | THR210 | |
| B | ARG115 |
