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 | 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 | 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: BINDING => ECO:0000269|PubMed:27997715, ECO:0007744|PDB:5GSN, ECO:0007744|PDB:5IPY, ECO:0007744|PDB:5IQ1, ECO:0007744|PDB:5IQ4 |
Chain | Residue | Details |
A | SER13 | |
A | SER208 | |
A | ARG229 | |
A | GLN318 | |
A | THR321 | |
B | SER13 | |
B | GLU38 | |
B | GLN40 | |
B | LEU46 | |
B | TRP47 | |
B | HIS63 | |
A | GLU38 | |
B | VAL126 | |
B | TYR173 | |
B | SER206 | |
B | SER208 | |
B | ARG229 | |
B | GLN318 | |
B | THR321 | |
A | GLN40 | |
A | LEU46 | |
A | TRP47 | |
A | HIS63 | |
A | VAL126 | |
A | TYR173 | |
A | SER206 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27997715, ECO:0007744|PDB:5IPY, ECO:0007744|PDB:5IQ1 |
Chain | Residue | Details |
A | TRP71 | |
A | ARG413 | |
B | TRP71 | |
B | ARG413 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27997715, ECO:0007744|PDB:5IPY, ECO:0007744|PDB:5IQ1, ECO:0007744|PDB:5IQ4 |
Chain | Residue | Details |
A | ASN73 | |
B | ASN73 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27997715, ECO:0007744|PDB:5GSN, ECO:0007744|PDB:5IPY, ECO:0007744|PDB:5IQ4 |
Chain | Residue | Details |
A | ALA205 | |
B | ALA205 |