5NMW
Crystal Structure of the pyrrolizidine alkaloid N-oxygenase from Zonocerus variegatus in complex with FAD
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 | 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 | 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 | 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 | 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 500 |
Chain | Residue |
A | GLY8 |
A | TYR56 |
A | SER58 |
A | LEU63 |
A | VAL65 |
A | ASN66 |
A | MET72 |
A | HIS113 |
A | HIS114 |
A | VAL115 |
A | CYS148 |
A | GLY10 |
A | THR149 |
A | TYR307 |
A | PHE311 |
A | HOH627 |
A | HOH649 |
A | HOH650 |
A | HOH683 |
A | HOH685 |
A | HOH688 |
A | HOH696 |
A | PRO11 |
A | HOH703 |
A | HOH731 |
A | HOH733 |
A | HOH750 |
A | HOH754 |
A | HOH770 |
A | HOH835 |
A | HOH847 |
A | SER12 |
A | GLU31 |
A | ARG32 |
A | GLY38 |
A | THR39 |
A | TRP40 |
site_id | AC2 |
Number of Residues | 35 |
Details | binding site for residue FAD B 501 |
Chain | Residue |
B | GLY8 |
B | GLY10 |
B | PRO11 |
B | SER12 |
B | GLU31 |
B | ARG32 |
B | GLY38 |
B | THR39 |
B | TRP40 |
B | TYR56 |
B | LEU63 |
B | VAL65 |
B | ASN66 |
B | MET72 |
B | HIS113 |
B | HIS114 |
B | VAL115 |
B | CYS148 |
B | THR149 |
B | GLY150 |
B | TYR307 |
B | PHE311 |
B | HOH634 |
B | HOH656 |
B | HOH658 |
B | HOH667 |
B | HOH679 |
B | HOH694 |
B | HOH735 |
B | HOH751 |
B | HOH752 |
B | HOH773 |
B | HOH799 |
B | HOH805 |
B | HOH843 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue MG B 502 |
Chain | Residue |
A | HOH724 |
A | HOH745 |
B | GLU368 |
B | ALA372 |
B | HOH604 |
B | HOH629 |
B | HOH711 |
B | HOH875 |
site_id | AC4 |
Number of Residues | 36 |
Details | binding site for residue FAD C 501 |
Chain | Residue |
C | TYR307 |
C | PHE311 |
C | HOH614 |
C | HOH629 |
C | HOH644 |
C | HOH645 |
C | HOH656 |
C | HOH659 |
C | HOH663 |
C | HOH673 |
C | HOH692 |
C | HOH705 |
C | HOH707 |
C | HOH716 |
C | HOH776 |
C | HOH779 |
C | HOH797 |
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 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | GLU368 |
C | HOH607 |
C | HOH655 |
C | HOH683 |
C | HOH724 |
D | HOH632 |
D | HOH728 |
site_id | AC6 |
Number of Residues | 34 |
Details | binding site for residue FAD D 500 |
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 | MET72 |
D | HIS113 |
D | HIS114 |
D | VAL115 |
D | CYS148 |
D | THR149 |
D | GLY150 |
D | TYR307 |
D | PHE311 |
D | HOH642 |
D | HOH646 |
D | HOH664 |
D | HOH666 |
D | HOH672 |
D | HOH675 |
D | HOH676 |
D | HOH692 |
D | HOH716 |
D | HOH730 |
D | HOH738 |
D | HOH789 |