3FMW
The crystal structure of MtmOIV, a Baeyer-Villiger monooxygenase from the mithramycin biosynthetic pathway in Streptomyces argillaceus.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| C | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD A 534 |
| Chain | Residue |
| A | GLY19 |
| A | ALA53 |
| A | ALA55 |
| A | GLN110 |
| A | GLU133 |
| A | VAL134 |
| A | ASP166 |
| A | GLY167 |
| A | THR171 |
| A | ILE191 |
| A | PHE272 |
| A | GLY21 |
| A | GLY291 |
| A | ASP292 |
| A | GLY302 |
| A | GLY304 |
| A | LEU305 |
| A | ASN306 |
| A | PRO22 |
| A | VAL23 |
| A | LEU41 |
| A | GLU42 |
| A | LYS43 |
| A | LEU44 |
| A | ARG52 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD B 534 |
| Chain | Residue |
| B | VAL18 |
| B | GLY19 |
| B | GLY21 |
| B | PRO22 |
| B | VAL23 |
| B | LEU41 |
| B | LYS43 |
| B | LEU44 |
| B | ARG52 |
| B | ALA53 |
| B | GLY54 |
| B | ALA55 |
| B | GLN110 |
| B | VAL134 |
| B | ASP166 |
| B | GLY167 |
| B | THR171 |
| B | PHE272 |
| B | ASP292 |
| B | PRO299 |
| B | GLY302 |
| B | GLY304 |
| B | LEU305 |
| B | ASN306 |
| B | EDO535 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD C 534 |
| Chain | Residue |
| C | VAL18 |
| C | GLY19 |
| C | GLY21 |
| C | PRO22 |
| C | VAL23 |
| C | LEU41 |
| C | GLU42 |
| C | LYS43 |
| C | LEU44 |
| C | ARG52 |
| C | ALA53 |
| C | GLY54 |
| C | ALA55 |
| C | GLN110 |
| C | VAL134 |
| C | ASP166 |
| C | GLY167 |
| C | THR171 |
| C | PHE272 |
| C | ASP292 |
| C | PRO299 |
| C | GLY302 |
| C | GLY304 |
| C | LEU305 |
| C | ASN306 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 535 |
| Chain | Residue |
| B | ASP292 |
| B | HIS297 |
| B | FAD534 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 535 |
| Chain | Residue |
| A | PRO299 |
| A | ILE300 |
