4PXH
Structure of P450sky (CYP163B3), a cytochrome P450 from skyllamycin biosynthesis in complex with a peptidyl carrier protein domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 | 0031177 | molecular_function | phosphopantetheine binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| 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 | 0031177 | molecular_function | phosphopantetheine binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| 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 | 0031177 | molecular_function | phosphopantetheine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | TYR66 |
| A | GLY248 |
| A | THR251 |
| A | SER252 |
| A | LEU288 |
| A | PRO293 |
| A | PHE297 |
| A | ARG299 |
| A | THR349 |
| A | PHE350 |
| A | GLY351 |
| A | ASN78 |
| A | HIS355 |
| A | CYS357 |
| A | GLY359 |
| A | HOH603 |
| A | HOH611 |
| B | KH4101 |
| A | LEU95 |
| A | ALA96 |
| A | HIS103 |
| A | ARG107 |
| A | PHE114 |
| A | LEU244 |
| A | GLY247 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE KH4 B 101 |
| Chain | Residue |
| A | ASP88 |
| A | SER89 |
| A | MET94 |
| A | LEU180 |
| A | TRP193 |
| A | TYR242 |
| A | GLY247 |
| A | THR251 |
| A | PHE297 |
| A | HEM501 |
| B | HIS41 |
| B | SER42 |
| B | HOH202 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | TYR66 |
| C | ASN78 |
| C | LEU95 |
| C | ALA96 |
| C | HIS103 |
| C | ARG107 |
| C | PHE114 |
| C | LEU244 |
| C | GLY247 |
| C | GLY248 |
| C | THR251 |
| C | SER252 |
| C | SER255 |
| C | LEU288 |
| C | PRO293 |
| C | PHE297 |
| C | ARG299 |
| C | THR349 |
| C | PHE350 |
| C | GLY351 |
| C | HIS355 |
| C | CYS357 |
| C | GLY359 |
| C | HOH605 |
| C | HOH606 |
| D | KH4101 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE KH4 D 101 |
| Chain | Residue |
| C | THR82 |
| C | ASP88 |
| C | SER89 |
| C | MET94 |
| C | LEU180 |
| C | TRP193 |
| C | ARG196 |
| C | TYR242 |
| C | LEU246 |
| C | GLY247 |
| C | THR251 |
| C | PHE297 |
| C | HEM501 |
| C | HOH616 |
| D | HIS41 |
| D | SER42 |
| D | HOH203 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM E 501 |
| Chain | Residue |
| E | GLY351 |
| E | HIS355 |
| E | CYS357 |
| E | GLY359 |
| E | HOH601 |
| F | KH4101 |
| E | TYR66 |
| E | ASN78 |
| E | LEU95 |
| E | ALA96 |
| E | HIS103 |
| E | ARG107 |
| E | PHE114 |
| E | LEU244 |
| E | GLY247 |
| E | GLY248 |
| E | THR251 |
| E | SER252 |
| E | LEU288 |
| E | PRO293 |
| E | PHE297 |
| E | ARG299 |
| E | THR349 |
| E | PHE350 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE KH4 F 101 |
| Chain | Residue |
| E | THR82 |
| E | ASP88 |
| E | SER89 |
| E | ALA90 |
| E | MET94 |
| E | LEU180 |
| E | TRP193 |
| E | LEU239 |
| E | TYR242 |
| E | GLY247 |
| E | THR251 |
| E | PHE297 |
| E | HEM501 |
| E | HOH615 |
| F | SER42 |
Functional Information from PROSITE/UniProt
