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