6XA2
Structure of the tirandamycin C-bound P450 monooxygenase TamI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| F | 0020037 | molecular_function | heme binding |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0004497 | molecular_function | monooxygenase activity |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| G | 0020037 | molecular_function | heme binding |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0005506 | molecular_function | iron ion binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| H | 0020037 | molecular_function | heme binding |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | MET100 |
| A | THR256 |
| A | LEU295 |
| A | ALA298 |
| A | THR299 |
| A | ARG301 |
| A | LEU324 |
| A | ALA351 |
| A | PHE352 |
| A | GLY353 |
| A | ILE356 |
| A | LEU101 |
| A | HIS357 |
| A | CYS359 |
| A | GLY361 |
| A | ALA365 |
| A | HIS108 |
| A | ARG112 |
| A | ILE163 |
| A | LEU244 |
| A | GLY248 |
| A | GLY249 |
| A | THR252 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue V0A A 502 |
| Chain | Residue |
| A | PHE92 |
| A | LEU101 |
| A | VAL185 |
| A | GLY248 |
| A | GLU251 |
| A | THR252 |
| A | LEU295 |
| A | THR299 |
| A | SER397 |
| A | THR398 |
| A | LEU399 |
| A | ILE400 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | MET100 |
| B | LEU101 |
| B | HIS108 |
| B | ARG112 |
| B | ILE163 |
| B | LEU244 |
| B | GLY249 |
| B | THR252 |
| B | THR256 |
| B | ALA298 |
| B | THR299 |
| B | ARG301 |
| B | LEU324 |
| B | ALA351 |
| B | PHE352 |
| B | GLY353 |
| B | ILE356 |
| B | HIS357 |
| B | CYS359 |
| B | GLY361 |
| B | LEU364 |
| B | ALA365 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue V0A B 502 |
| Chain | Residue |
| B | VAL42 |
| B | PRO43 |
| B | VAL44 |
| B | ALA91 |
| B | PHE92 |
| B | LEU101 |
| B | LEU184 |
| B | VAL185 |
| B | GLY248 |
| B | THR252 |
| B | THR299 |
| B | SER397 |
| B | THR398 |
| B | LEU399 |
| B | ILE400 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue HEM C 501 |
| Chain | Residue |
| C | MET100 |
| C | LEU101 |
| C | HIS108 |
| C | ARG112 |
| C | PHE119 |
| C | ILE163 |
| C | LEU244 |
| C | GLY248 |
| C | GLY249 |
| C | THR252 |
| C | THR256 |
| C | LEU289 |
| C | ALA298 |
| C | THR299 |
| C | ARG301 |
| C | ALA351 |
| C | PHE352 |
| C | GLY353 |
| C | ILE356 |
| C | HIS357 |
| C | CYS359 |
| C | GLY361 |
| C | ALA365 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue V0A C 502 |
| Chain | Residue |
| C | VAL185 |
| C | GLY248 |
| C | GLU251 |
| C | THR252 |
| C | LEU295 |
| C | THR299 |
| C | SER397 |
| C | THR398 |
| C | LEU399 |
| C | ILE400 |
| C | ALA91 |
| C | PHE92 |
| C | LEU101 |
| C | LEU184 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue HEM D 501 |
| Chain | Residue |
| D | MET100 |
| D | LEU101 |
| D | HIS108 |
| D | ARG112 |
| D | PHE119 |
| D | ILE163 |
| D | LEU244 |
| D | GLY249 |
| D | THR252 |
| D | THR256 |
| D | LEU295 |
| D | ALA298 |
| D | THR299 |
| D | ARG301 |
| D | LEU324 |
| D | ALA351 |
| D | PHE352 |
| D | GLY353 |
| D | ILE356 |
| D | HIS357 |
| D | CYS359 |
| D | GLY361 |
| D | ALA365 |
| D | V0A502 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue V0A D 502 |
| Chain | Residue |
| D | ALA91 |
| D | PHE92 |
| D | LEU101 |
| D | LEU184 |
| D | VAL185 |
| D | ILE247 |
| D | GLY248 |
| D | GLU251 |
| D | THR252 |
| D | THR299 |
| D | SER397 |
| D | THR398 |
| D | LEU399 |
| D | ILE400 |
| D | HEM501 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | binding site for residue HEM E 501 |
| Chain | Residue |
| E | MET100 |
| E | LEU101 |
| E | HIS108 |
| E | ARG112 |
| E | PHE119 |
| E | ILE163 |
| E | LEU244 |
| E | GLY248 |
| E | GLY249 |
| E | THR252 |
| E | THR256 |
| E | LEU295 |
| E | ALA298 |
| E | THR299 |
| E | ARG301 |
| E | ALA351 |
| E | PHE352 |
| E | GLY353 |
| E | ILE356 |
| E | HIS357 |
| E | CYS359 |
| E | GLY361 |
| E | ALA365 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue V0A E 502 |
| Chain | Residue |
| E | ALA91 |
| E | PHE92 |
| E | LEU101 |
| E | LEU184 |
| E | VAL185 |
| E | GLY248 |
| E | THR252 |
| E | LEU295 |
| E | THR299 |
| E | SER397 |
| E | THR398 |
| E | LEU399 |
| E | ILE400 |
| site_id | AD2 |
| Number of Residues | 23 |
| Details | binding site for residue HEM F 501 |
| Chain | Residue |
| F | MET100 |
| F | LEU101 |
| F | HIS108 |
| F | ARG112 |
| F | PHE119 |
| F | LEU244 |
| F | GLY249 |
| F | THR252 |
| F | THR256 |
| F | LEU295 |
| F | ALA298 |
| F | THR299 |
| F | ARG301 |
| F | ALA351 |
| F | PHE352 |
| F | GLY353 |
| F | ILE356 |
| F | HIS357 |
| F | CYS359 |
| F | GLY361 |
| F | LEU364 |
| F | ALA365 |
| F | V0A502 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue V0A F 502 |
| Chain | Residue |
| F | VAL44 |
| F | ALA91 |
| F | PHE92 |
| F | LEU101 |
| F | LEU184 |
| F | VAL185 |
| F | GLY248 |
| F | THR252 |
| F | LEU295 |
| F | THR299 |
| F | SER397 |
| F | THR398 |
| F | LEU399 |
| F | ILE400 |
| F | HEM501 |
| site_id | AD4 |
| Number of Residues | 25 |
| Details | binding site for residue HEM G 501 |
| Chain | Residue |
| G | MET100 |
| G | LEU101 |
| G | HIS108 |
| G | ARG112 |
| G | ILE163 |
| G | LEU244 |
| G | GLY248 |
| G | GLY249 |
| G | THR252 |
| G | THR256 |
| G | LEU295 |
| G | ALA298 |
| G | THR299 |
| G | ARG301 |
| G | LEU324 |
| G | ALA351 |
| G | PHE352 |
| G | GLY353 |
| G | ILE356 |
| G | HIS357 |
| G | CYS359 |
| G | GLY361 |
| G | LEU364 |
| G | ALA365 |
| G | V0A502 |
| site_id | AD5 |
| Number of Residues | 15 |
| Details | binding site for residue V0A G 502 |
| Chain | Residue |
| G | VAL44 |
| G | ALA91 |
| G | PHE92 |
| G | LEU101 |
| G | LEU184 |
| G | VAL185 |
| G | ILE247 |
| G | THR252 |
| G | LEU295 |
| G | THR299 |
| G | SER397 |
| G | THR398 |
| G | LEU399 |
| G | ILE400 |
| G | HEM501 |
| site_id | AD6 |
| Number of Residues | 21 |
| Details | binding site for residue HEM H 501 |
| Chain | Residue |
| H | MET100 |
| H | LEU101 |
| H | HIS108 |
| H | ARG112 |
| H | LEU245 |
| H | GLY248 |
| H | GLY249 |
| H | THR252 |
| H | THR256 |
| H | LEU289 |
| H | ALA298 |
| H | THR299 |
| H | ARG301 |
| H | ALA351 |
| H | PHE352 |
| H | GLY353 |
| H | ILE356 |
| H | HIS357 |
| H | CYS359 |
| H | GLY361 |
| H | ALA365 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for residue V0A H 502 |
| Chain | Residue |
| H | PHE92 |
| H | LEU101 |
| H | VAL185 |
| H | GLY248 |
| H | THR252 |
| H | LEU295 |
| H | THR299 |
| H | SER397 |
| H | THR398 |
| H | LEU399 |
| H | ILE400 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHYCLG |
| Chain | Residue | Details |
| A | PHE352-GLY361 |
