4ATD
Crystal structure of native Raucaffricine glucosidase
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 | 0016787 | molecular_function | hydrolase 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 | 0016787 | molecular_function | hydrolase 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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1514 |
| Chain | Residue |
| B | TYR481 |
| B | GLY482 |
| B | ARG484 |
| B | TYR492 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1514 |
| Chain | Residue |
| A | TYR481 |
| A | GLY482 |
| A | ARG484 |
| A | TYR492 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1515 |
| Chain | Residue |
| A | TYR481 |
| A | TYR492 |
| A | PHE496 |
| A | HOH2054 |
| A | ALA71 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1516 |
| Chain | Residue |
| A | ASP425 |
| A | GLU435 |
| A | ALA436 |
| A | LYS438 |
| A | ASP439 |
| A | HOH2209 |
| A | HOH2210 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1515 |
| Chain | Residue |
| B | ASP425 |
| B | LEU431 |
| B | GLU435 |
| B | ALA436 |
| B | LYS438 |
| B | ASP439 |
| B | HOH2206 |
| B | HOH2208 |
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 | 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":"UniProtKB","id":"Q7XSK0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22004291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22704651","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3U5Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ATL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EK7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22004291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22704651","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3ZJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ATL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EK7","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":"PubMed","id":"22004291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22704651","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3U5Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZJ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EK7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q1XH05","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Directs the conformation of W-392"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Controls the gate shape and acceptance of substrates"} |
| Chain | Residue | Details |
