2JBS
Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0052881 | molecular_function | 4-hydroxyphenylacetate 3-monooxygenase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0052881 | molecular_function | 4-hydroxyphenylacetate 3-monooxygenase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| C | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0052881 | molecular_function | 4-hydroxyphenylacetate 3-monooxygenase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0052881 | molecular_function | 4-hydroxyphenylacetate 3-monooxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN A1423 |
| Chain | Residue |
| A | TRP112 |
| A | HIS396 |
| A | ALA397 |
| D | ARG292 |
| D | TYR296 |
| D | GLY373 |
| D | ALA374 |
| D | THR375 |
| A | LEU116 |
| A | SER146 |
| A | SER147 |
| A | ILE148 |
| A | TRP169 |
| A | SER170 |
| A | SER171 |
| A | SER220 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN B1423 |
| Chain | Residue |
| B | TRP112 |
| B | LEU116 |
| B | SER146 |
| B | SER147 |
| B | ILE148 |
| B | TRP169 |
| B | SER170 |
| B | SER171 |
| B | MET392 |
| B | HIS396 |
| B | ALA397 |
| C | ARG292 |
| C | TYR296 |
| C | GLY373 |
| C | ALA374 |
| C | THR375 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN C1423 |
| Chain | Residue |
| B | ARG292 |
| B | TYR296 |
| B | GLY373 |
| B | ALA374 |
| B | THR375 |
| C | TRP112 |
| C | LEU116 |
| C | SER146 |
| C | SER147 |
| C | ILE148 |
| C | TRP169 |
| C | SER170 |
| C | SER171 |
| C | SER220 |
| C | HIS396 |
| C | ALA397 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN D1423 |
| Chain | Residue |
| A | ARG292 |
| A | ALA295 |
| A | TYR296 |
| A | GLY373 |
| A | ALA374 |
| A | THR375 |
| D | TRP112 |
| D | LEU116 |
| D | SER146 |
| D | SER147 |
| D | ILE148 |
| D | TRP169 |
| D | SER170 |
| D | SER171 |
| D | HIS396 |
| D | ALA397 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17227849","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | PHE266 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | THR260 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | THR260 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | THR260 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | PHE266 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | PHE266 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | PHE266 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | ALA397 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | ALA397 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | ALA397 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | ALA397 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | THR260 |
