4ATL
Crystal structure of Raucaffricine glucosidase in complex with Glucose
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 | 0016740 | molecular_function | transferase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0050247 | molecular_function | raucaffricine beta-glucosidase activity |
| A | 0050506 | molecular_function | vomilenine glucosyltransferase 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 | 0016740 | molecular_function | transferase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0050247 | molecular_function | raucaffricine beta-glucosidase activity |
| B | 0050506 | molecular_function | vomilenine glucosyltransferase 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. FiMGtGsSAYQiEgG |
| Chain | Residue | Details |
| A | PHE26-GLY40 |
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 | GLU186 | |
| B | GLU186 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q7XSK0 |
| Chain | Residue | Details |
| A | GLU420 | |
| B | GLU420 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22004291, ECO:0000305|PubMed:22704651, ECO:0007744|PDB:3U5Y, ECO:0007744|PDB:3ZJ6, ECO:0007744|PDB:4ATL, ECO:0007744|PDB:4EK7 |
| Chain | Residue | Details |
| A | GLN36 | |
| A | ASN185 | |
| A | GLU420 | |
| A | GLU476 | |
| B | GLN36 | |
| B | ASN185 | |
| B | GLU420 | |
| B | GLU476 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22004291, ECO:0000305|PubMed:22704651, ECO:0007744|PDB:3ZJ6, ECO:0007744|PDB:4ATL, ECO:0007744|PDB:4EK7 |
| Chain | Residue | Details |
| A | HIS140 | |
| B | HIS140 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8L7J2 |
| Chain | Residue | Details |
| A | TYR347 | |
| B | TYR347 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22004291, ECO:0000305|PubMed:22704651, ECO:0007744|PDB:3U5Y, ECO:0007744|PDB:3ZJ6, ECO:0007744|PDB:4EK7 |
| Chain | Residue | Details |
| A | TRP469 | |
| B | TRP469 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q1XH05 |
| Chain | Residue | Details |
| A | PHE485 | |
| B | PHE485 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Directs the conformation of W-392 |
| Chain | Residue | Details |
| A | SER390 | |
| B | SER390 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | SITE: Controls the gate shape and acceptance of substrates |
| Chain | Residue | Details |
| A | TRP392 | |
| B | TRP392 |
