6NEV
FAD-dependent monooxygenase TropB from T. stipitatus Y239F 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 | 27 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY19 |
| A | ARG124 |
| A | LYS144 |
| A | ARG145 |
| A | LEU146 |
| A | ALA176 |
| A | ASP177 |
| A | ARG182 |
| A | ASP322 |
| A | GLY332 |
| A | ALA333 |
| A | GLY21 |
| A | GLY334 |
| A | ALA335 |
| A | CYS336 |
| A | CL502 |
| A | HOH615 |
| A | HOH617 |
| A | HOH618 |
| A | HOH636 |
| A | ILE22 |
| A | ILE23 |
| A | PHE41 |
| A | GLU42 |
| A | GLN43 |
| A | MET54 |
| A | ALA55 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | PRO329 |
| A | ALA333 |
| A | GLY334 |
| A | FAD501 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | VAL18 |
| B | GLY19 |
| B | GLY21 |
| B | ILE22 |
| B | ILE23 |
| B | PHE41 |
| B | GLU42 |
| B | GLN43 |
| B | GLU49 |
| B | MET54 |
| B | ALA55 |
| B | ARG124 |
| B | LYS144 |
| B | ARG145 |
| B | LEU146 |
| B | ALA176 |
| B | ASP177 |
| B | GLY178 |
| B | ARG182 |
| B | ARG206 |
| B | GLY321 |
| B | ASP322 |
| B | GLY332 |
| B | ALA333 |
| B | GLY334 |
| B | ALA335 |
| B | CYS336 |
| B | CL502 |
| B | HOH601 |
| B | HOH608 |
| B | HOH612 |
| B | HOH619 |
| B | HOH628 |
| B | HOH652 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | PRO329 |
| B | GLY332 |
| B | ALA333 |
| B | GLY334 |
| B | FAD501 |
| B | HOH652 |
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 |
