2JBT
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 | 0009056 | biological_process | catabolic process |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
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 | 0009056 | biological_process | catabolic process |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
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 | 0009056 | biological_process | catabolic process |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
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 | 0009056 | biological_process | catabolic process |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
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 | 17 |
Details | BINDING SITE FOR RESIDUE FMN A1423 |
Chain | Residue |
A | TRP112 |
A | HIS396 |
A | ALA397 |
A | 4HP1424 |
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 | 10 |
Details | BINDING SITE FOR RESIDUE 4HP A1424 |
Chain | Residue |
A | LEU116 |
A | HIS120 |
A | SER146 |
A | ILE148 |
A | ARG263 |
A | PHE266 |
A | ALA267 |
A | TYR398 |
A | FMN1423 |
D | TYR296 |
site_id | AC3 |
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 | SER171 |
B | SER220 |
B | HIS396 |
B | ALA397 |
B | 4HP1424 |
C | ARG292 |
C | TYR296 |
C | GLY373 |
C | ALA374 |
C | THR375 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 4HP B1424 |
Chain | Residue |
B | LEU116 |
B | HIS120 |
B | SER146 |
B | ILE148 |
B | ARG263 |
B | PHE266 |
B | ALA267 |
B | TYR398 |
B | FMN1423 |
C | TYR296 |
site_id | AC5 |
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 | SER146 |
C | SER147 |
C | ILE148 |
C | TRP169 |
C | SER170 |
C | SER171 |
C | SER220 |
C | HIS396 |
C | ALA397 |
C | 4HP1424 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 4HP C1424 |
Chain | Residue |
B | TYR296 |
C | LEU116 |
C | HIS120 |
C | SER146 |
C | ILE148 |
C | ARG263 |
C | PHE266 |
C | ALA267 |
C | TYR398 |
C | FMN1423 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE FMN D1423 |
Chain | Residue |
A | ARG292 |
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 | SER220 |
D | HIS396 |
D | ALA397 |
D | 4HP1424 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 4HP D1424 |
Chain | Residue |
D | ILE148 |
D | ARG263 |
D | PHE266 |
D | ALA267 |
D | TYR398 |
D | FMN1423 |
D | LEU116 |
D | HIS120 |
D | SER146 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17227849 |
Chain | Residue | Details |
A | TRP112 | |
B | HIS396 | |
C | TRP112 | |
C | TRP169 | |
C | ARG292 | |
C | ALA374 | |
C | HIS396 | |
D | TRP112 | |
D | TRP169 | |
D | ARG292 | |
D | ALA374 | |
A | TRP169 | |
D | HIS396 | |
A | ARG292 | |
A | ALA374 | |
A | HIS396 | |
B | TRP112 | |
B | TRP169 | |
B | ARG292 | |
B | ALA374 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS120 | |
C | SER146 | |
C | ARG263 | |
C | TYR296 | |
D | HIS120 | |
D | SER146 | |
D | ARG263 | |
D | TYR296 | |
A | SER146 | |
A | ARG263 | |
A | TYR296 | |
B | HIS120 | |
B | SER146 | |
B | ARG263 | |
B | TYR296 | |
C | HIS120 |
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 |