6NEU
FAD-dependent monooxygenase TropB from T. stipitatus R206Q variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0044550 | biological_process | secondary metabolite biosynthetic process |
| A | 0071949 | molecular_function | FAD binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0044550 | biological_process | secondary metabolite biosynthetic process |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY19 |
| A | ALA55 |
| A | ARG124 |
| A | LYS144 |
| A | ARG145 |
| A | LEU146 |
| A | ALA176 |
| A | ASP177 |
| A | GLY178 |
| A | ASP322 |
| A | PRO329 |
| A | GLY21 |
| A | GLY332 |
| A | ALA333 |
| A | GLY334 |
| A | ALA335 |
| A | CYS336 |
| A | CL502 |
| A | HOH603 |
| A | HOH612 |
| A | HOH620 |
| A | HOH629 |
| A | ILE22 |
| A | HOH642 |
| A | HOH645 |
| A | ILE23 |
| A | PHE41 |
| A | GLU42 |
| A | GLN43 |
| A | GLU49 |
| A | MET54 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | PRO329 |
| A | ALA333 |
| A | GLY334 |
| A | FAD501 |
| A | HOH643 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | GLY19 |
| B | GLY21 |
| B | ILE22 |
| B | ILE23 |
| B | PHE41 |
| B | GLU42 |
| B | GLN43 |
| B | MET54 |
| B | ALA55 |
| B | ARG124 |
| B | LYS144 |
| B | ARG145 |
| B | LEU146 |
| B | ALA176 |
| B | ASP177 |
| B | GLY178 |
| B | ARG182 |
| B | GLY321 |
| B | ASP322 |
| B | GLY332 |
| B | ALA333 |
| B | GLY334 |
| B | ALA335 |
| B | CYS336 |
| B | CL502 |
| B | HOH601 |
| B | HOH607 |
| B | HOH608 |
| B | HOH611 |
| B | HOH613 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | PRO329 |
| B | ALA333 |
| B | GLY334 |
| B | FAD501 |
| B | HOH652 |
| B | HOH659 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | TYR305 |
| B | ASP388 |
| B | ARG391 |
| B | ARG392 |
| B | ASP395 |
| B | HOH670 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"31346489","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31346489","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NET","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6NEU","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6NES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NEV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31346489","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NEV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
