5IQ1
Crystal structure of RnTmm mutant Y207S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0034899 | molecular_function | trimethylamine monooxygenase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP 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 | 0034899 | molecular_function | trimethylamine monooxygenase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NAP A 501 |
| Chain | Residue |
| A | TYR67 |
| A | SER207 |
| A | SER208 |
| A | ASP211 |
| A | ARG229 |
| A | SER230 |
| A | CYS271 |
| A | THR272 |
| A | GLY273 |
| A | ARG413 |
| A | FAD502 |
| A | TRP71 |
| A | HOH601 |
| A | HOH603 |
| A | HOH607 |
| A | HOH611 |
| A | HOH642 |
| A | HOH645 |
| A | HOH667 |
| A | HOH796 |
| A | HOH828 |
| A | HOH846 |
| A | ASN73 |
| A | HOH900 |
| A | HOH922 |
| A | HOH959 |
| A | ASN169 |
| A | PRO171 |
| A | TYR173 |
| A | MET203 |
| A | ALA205 |
| A | SER206 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for residue FAD A 502 |
| Chain | Residue |
| A | GLY9 |
| A | GLY11 |
| A | PRO12 |
| A | SER13 |
| A | PHE37 |
| A | GLU38 |
| A | LYS39 |
| A | GLN40 |
| A | GLY45 |
| A | LEU46 |
| A | TRP47 |
| A | HIS63 |
| A | MET66 |
| A | SER72 |
| A | ASN73 |
| A | LEU79 |
| A | PRO125 |
| A | VAL126 |
| A | ALA161 |
| A | SER162 |
| A | GLY163 |
| A | PHE165 |
| A | PHE280 |
| A | GLN318 |
| A | THR321 |
| A | PHE322 |
| A | NAP501 |
| A | HOH648 |
| A | HOH727 |
| A | HOH751 |
| A | HOH768 |
| A | HOH782 |
| A | HOH818 |
| A | HOH821 |
| A | HOH936 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue NAP B 501 |
| Chain | Residue |
| B | TYR67 |
| B | TRP71 |
| B | ASN73 |
| B | PHE165 |
| B | ASN169 |
| B | PRO171 |
| B | TYR173 |
| B | MET203 |
| B | ALA205 |
| B | SER206 |
| B | SER207 |
| B | SER208 |
| B | ASP211 |
| B | ARG229 |
| B | SER230 |
| B | CYS271 |
| B | THR272 |
| B | GLY273 |
| B | ARG413 |
| B | FAD502 |
| B | HOH603 |
| B | HOH604 |
| B | HOH630 |
| B | HOH641 |
| B | HOH645 |
| B | HOH658 |
| B | HOH663 |
| B | HOH695 |
| B | HOH749 |
| B | HOH762 |
| B | HOH770 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | binding site for residue FAD B 502 |
| Chain | Residue |
| B | GLY11 |
| B | PRO12 |
| B | SER13 |
| B | PHE37 |
| B | GLU38 |
| B | LYS39 |
| B | GLN40 |
| B | GLY45 |
| B | LEU46 |
| B | TRP47 |
| B | HIS63 |
| B | SER72 |
| B | ASN73 |
| B | LEU79 |
| B | PRO125 |
| B | VAL126 |
| B | ALA161 |
| B | SER162 |
| B | GLY163 |
| B | PHE165 |
| B | PHE280 |
| B | GLN318 |
| B | THR321 |
| B | NAP501 |
| B | HOH621 |
| B | HOH676 |
| B | HOH677 |
| B | HOH718 |
| B | HOH723 |
| B | HOH796 |
| B | HOH812 |
| B | GLY9 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27997715","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GSN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IQ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IQ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27997715","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IQ1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27997715","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IQ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IQ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27997715","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GSN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IPY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IQ4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
