2XVE
Crystal structure of bacterial flavin-containing monooxygenase
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 | 0042802 | molecular_function | identical protein binding |
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 | 0042802 | molecular_function | identical protein binding |
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 | 0042802 | molecular_function | identical protein binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NO3 A 465 |
Chain | Residue |
A | HIS185 |
A | TYR274 |
A | HOH2150 |
A | ALA186 |
A | SER206 |
A | TYR207 |
A | SER208 |
A | ALA209 |
A | CYS271 |
A | THR272 |
A | GLY273 |
site_id | AC2 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD B 465 |
Chain | Residue |
B | GLY9 |
B | GLY11 |
B | PRO12 |
B | SER13 |
B | GLU38 |
B | LYS39 |
B | GLN40 |
B | GLY45 |
B | GLN46 |
B | TRP47 |
B | HIS63 |
B | MET66 |
B | SER72 |
B | ASN73 |
B | LEU79 |
B | THR124 |
B | ALA125 |
B | VAL126 |
B | CYS161 |
B | THR162 |
B | GLY163 |
B | PHE165 |
B | TYR207 |
B | SER208 |
B | GLN318 |
B | SER321 |
B | PHE322 |
B | PHE325 |
B | GOL468 |
B | HOH2020 |
B | HOH2066 |
B | HOH2067 |
B | HOH2143 |
B | HOH2149 |
B | HOH2233 |
B | HOH2234 |
B | HOH2322 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NO3 B 466 |
Chain | Residue |
B | HIS185 |
B | ALA186 |
B | SER206 |
B | TYR207 |
B | SER208 |
B | ALA209 |
B | CYS271 |
B | THR272 |
B | GLY273 |
B | TYR274 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO3 B 467 |
Chain | Residue |
B | TYR235 |
B | TRP319 |
B | TRP400 |
B | LYS401 |
B | LYS404 |
B | GOL469 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 468 |
Chain | Residue |
B | ASN73 |
B | GLY74 |
B | TYR207 |
B | GLN318 |
B | TRP319 |
B | PHE397 |
B | FAD465 |
B | GOL469 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 469 |
Chain | Residue |
B | ASP317 |
B | GLN318 |
B | NO3467 |
B | GOL468 |
site_id | AC7 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD C 465 |
Chain | Residue |
C | SER208 |
C | GLN318 |
C | SER321 |
C | PHE325 |
C | HOH2012 |
C | HOH2086 |
C | HOH2091 |
C | HOH2145 |
C | HOH2146 |
C | HOH2181 |
C | HOH2182 |
C | GLY9 |
C | GLY11 |
C | PRO12 |
C | SER13 |
C | GLU38 |
C | LYS39 |
C | GLN40 |
C | GLY45 |
C | GLN46 |
C | TRP47 |
C | HIS63 |
C | MET66 |
C | SER72 |
C | ASN73 |
C | LEU79 |
C | THR124 |
C | ALA125 |
C | VAL126 |
C | CYS161 |
C | THR162 |
C | GLY163 |
C | PHE165 |
C | TYR207 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NO3 C 466 |
Chain | Residue |
C | HIS185 |
C | ALA186 |
C | SER206 |
C | TYR207 |
C | SER208 |
C | ALA209 |
C | CYS271 |
C | THR272 |
C | GLY273 |
C | TYR274 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 467 |
Chain | Residue |
C | ASP317 |
C | GLN318 |
C | TRP319 |