5NMX
Crystal Structure of the pyrrolizidine alkaloid N-oxygenase from Zonocerus variegatus in complex with FAD and NADP+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 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 |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY8 |
| A | TYR56 |
| A | SER58 |
| A | VAL65 |
| A | ASN66 |
| A | MET72 |
| A | HIS113 |
| A | HIS114 |
| A | VAL115 |
| A | CYS148 |
| A | THR149 |
| A | GLY10 |
| A | GLY150 |
| A | THR152 |
| A | TYR307 |
| A | PHE311 |
| A | NAP502 |
| A | HOH617 |
| A | HOH638 |
| A | HOH645 |
| A | HOH654 |
| A | HOH657 |
| A | PRO11 |
| A | HOH661 |
| A | HOH710 |
| A | HOH717 |
| A | HOH728 |
| A | HOH761 |
| A | HOH772 |
| A | HOH779 |
| A | HOH841 |
| A | SER12 |
| A | GLU31 |
| A | ARG32 |
| A | GLY38 |
| A | THR39 |
| A | TRP40 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | binding site for residue NAP A 502 |
| Chain | Residue |
| A | TYR60 |
| A | PHE64 |
| A | ASN66 |
| A | PRO158 |
| A | VAL190 |
| A | GLY191 |
| A | GLY193 |
| A | PRO194 |
| A | SER195 |
| A | SER213 |
| A | LYS215 |
| A | CYS258 |
| A | THR259 |
| A | GLY260 |
| A | TYR307 |
| A | ARG398 |
| A | FAD501 |
| A | HOH611 |
| A | HOH620 |
| A | HOH628 |
| A | HOH633 |
| A | HOH659 |
| A | HOH678 |
| A | HOH685 |
| A | HOH689 |
| A | HOH739 |
| A | HOH788 |
| A | HOH795 |
| A | HOH821 |
| A | HOH876 |
| A | HOH893 |
| site_id | AC3 |
| Number of Residues | 38 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | HOH771 |
| B | HOH777 |
| B | HOH782 |
| B | HOH788 |
| B | HOH789 |
| B | HOH857 |
| B | HOH866 |
| B | GLY8 |
| B | GLY10 |
| B | PRO11 |
| B | SER12 |
| B | GLU31 |
| B | ARG32 |
| B | GLY38 |
| B | THR39 |
| B | TRP40 |
| B | TYR56 |
| B | SER58 |
| B | VAL65 |
| B | ASN66 |
| B | MET72 |
| B | HIS113 |
| B | HIS114 |
| B | VAL115 |
| B | CYS148 |
| B | THR149 |
| B | GLY150 |
| B | THR152 |
| B | TYR307 |
| B | PHE311 |
| B | NAP502 |
| B | HOH644 |
| B | HOH647 |
| B | HOH671 |
| B | HOH674 |
| B | HOH677 |
| B | HOH680 |
| B | HOH744 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | binding site for residue NAP B 502 |
| Chain | Residue |
| B | TYR60 |
| B | PHE64 |
| B | ASN66 |
| B | PRO158 |
| B | VAL190 |
| B | GLY191 |
| B | GLY193 |
| B | PRO194 |
| B | SER195 |
| B | ASP198 |
| B | SER213 |
| B | ARG214 |
| B | LYS215 |
| B | CYS258 |
| B | THR259 |
| B | GLY260 |
| B | TYR261 |
| B | ARG398 |
| B | FAD501 |
| B | HOH605 |
| B | HOH607 |
| B | HOH617 |
| B | HOH619 |
| B | HOH624 |
| B | HOH625 |
| B | HOH631 |
| B | HOH654 |
| B | HOH675 |
| B | HOH682 |
| B | HOH695 |
| B | HOH711 |
| B | HOH746 |
| B | HOH773 |
| B | HOH814 |
| B | HOH867 |
| B | HOH903 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | HOH718 |
| B | HOH795 |
| B | HOH980 |
| B | HOH987 |
| B | HOH988 |
| site_id | AC6 |
| Number of Residues | 37 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | GLY8 |
| C | GLY10 |
| C | PRO11 |
| C | SER12 |
| C | GLU31 |
| C | ARG32 |
| C | GLY38 |
| C | THR39 |
| C | TRP40 |
| C | TYR56 |
| C | LEU63 |
| C | VAL65 |
| C | ASN66 |
| C | MET72 |
| C | HIS113 |
| C | HIS114 |
| C | VAL115 |
| C | CYS148 |
| C | THR149 |
| C | GLY150 |
| C | TYR307 |
| C | PHE311 |
| C | NAP502 |
| C | HOH682 |
| C | HOH685 |
| C | HOH692 |
| C | HOH698 |
| C | HOH704 |
| C | HOH711 |
| C | HOH758 |
| C | HOH770 |
| C | HOH776 |
| C | HOH785 |
| C | HOH797 |
| C | HOH822 |
| C | HOH829 |
| C | HOH856 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for residue NAP C 502 |
| Chain | Residue |
| C | TYR60 |
| C | LEU63 |
| C | PHE64 |
| C | ASN66 |
| C | PRO158 |
| C | VAL190 |
| C | GLY191 |
| C | GLY193 |
| C | PRO194 |
| C | SER195 |
| C | ASP198 |
| C | SER213 |
| C | LYS215 |
| C | CYS258 |
| C | THR259 |
| C | ARG398 |
| C | FAD501 |
| C | HOH601 |
| C | HOH615 |
| C | HOH616 |
| C | HOH620 |
| C | HOH625 |
| C | HOH637 |
| C | HOH675 |
| C | HOH690 |
| C | HOH705 |
| C | HOH819 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 503 |
| Chain | Residue |
| A | HOH704 |
| A | HOH832 |
| A | HOH932 |
| C | HOH624 |
| C | HOH694 |
| C | HOH702 |
| site_id | AC9 |
| Number of Residues | 37 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| D | GLY8 |
| D | GLY10 |
| D | PRO11 |
| D | SER12 |
| D | GLU31 |
| D | ARG32 |
| D | GLY38 |
| D | THR39 |
| D | TRP40 |
| D | TYR56 |
| D | LEU63 |
| D | VAL65 |
| D | ASN66 |
| D | LEU67 |
| D | MET72 |
| D | HIS113 |
| D | HIS114 |
| D | VAL115 |
| D | CYS148 |
| D | THR149 |
| D | GLY150 |
| D | THR152 |
| D | TYR307 |
| D | NAP502 |
| D | HOH640 |
| D | HOH647 |
| D | HOH651 |
| D | HOH654 |
| D | HOH674 |
| D | HOH713 |
| D | HOH715 |
| D | HOH717 |
| D | HOH728 |
| D | HOH749 |
| D | HOH756 |
| D | HOH798 |
| D | HOH822 |
| site_id | AD1 |
| Number of Residues | 29 |
| Details | binding site for residue NAP D 502 |
| Chain | Residue |
| D | TYR60 |
| D | LEU63 |
| D | PHE64 |
| D | ASN66 |
| D | PRO158 |
| D | VAL190 |
| D | GLY191 |
| D | GLY193 |
| D | PRO194 |
| D | SER195 |
| D | SER213 |
| D | LYS215 |
| D | CYS258 |
| D | THR259 |
| D | GLY260 |
| D | TYR261 |
| D | HIS351 |
| D | ARG398 |
| D | FAD501 |
| D | HOH610 |
| D | HOH614 |
| D | HOH637 |
| D | HOH672 |
| D | HOH690 |
| D | HOH716 |
| D | HOH719 |
| D | HOH738 |
| D | HOH781 |
| D | HOH796 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 503 |
| Chain | Residue |
| B | HOH691 |
| B | HOH772 |
| D | HOH611 |
| D | HOH671 |
| D | HOH815 |
| D | HOH893 |
