6DLL
2.2 Angstrom Resolution Crystal Structure of P-Hydroxybenzoate Hydroxylase from Pseudomonas putida in Complex with FAD.
Replaces: 5TTIFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0018659 | molecular_function | 4-hydroxybenzoate 3-monooxygenase activity |
| A | 0018874 | biological_process | benzoate metabolic process |
| A | 0043639 | biological_process | benzoate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0018659 | molecular_function | 4-hydroxybenzoate 3-monooxygenase activity |
| B | 0018874 | biological_process | benzoate metabolic process |
| B | 0043639 | biological_process | benzoate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 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 |
| C | 0018659 | molecular_function | 4-hydroxybenzoate 3-monooxygenase activity |
| C | 0018874 | biological_process | benzoate metabolic process |
| C | 0043639 | biological_process | benzoate catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 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 |
| D | 0018659 | molecular_function | 4-hydroxybenzoate 3-monooxygenase activity |
| D | 0018874 | biological_process | benzoate metabolic process |
| D | 0043639 | biological_process | benzoate catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | GLY9 |
| A | ALA45 |
| A | GLN102 |
| A | CYS158 |
| A | ASP159 |
| A | GLY160 |
| A | GLY163 |
| A | ILE164 |
| A | TYR222 |
| A | GLY285 |
| A | ASP286 |
| A | GLY11 |
| A | PRO293 |
| A | GLY298 |
| A | LEU299 |
| A | HOH510 |
| A | HOH525 |
| A | HOH543 |
| A | HOH546 |
| A | HOH549 |
| A | HOH554 |
| A | HOH556 |
| A | PRO12 |
| A | HOH559 |
| A | HOH562 |
| A | HOH570 |
| A | HOH641 |
| A | HOH643 |
| A | HOH659 |
| A | SER13 |
| A | GLU32 |
| A | ARG33 |
| A | GLN34 |
| A | ARG42 |
| A | ARG44 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | LEU301 |
| A | ARG335 |
| A | GLY339 |
| A | LEU389 |
| A | HOH589 |
| A | HOH697 |
| site_id | AC3 |
| Number of Residues | 37 |
| Details | binding site for residue FAD B 401 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | PRO12 |
| B | SER13 |
| B | VAL31 |
| B | GLU32 |
| B | ARG33 |
| B | GLN34 |
| B | VAL39 |
| B | ARG42 |
| B | ARG44 |
| B | ALA45 |
| B | GLN102 |
| B | CYS158 |
| B | ASP159 |
| B | GLY160 |
| B | GLY163 |
| B | ILE164 |
| B | TYR222 |
| B | GLY285 |
| B | ASP286 |
| B | PRO293 |
| B | GLY298 |
| B | LEU299 |
| B | HOH545 |
| B | HOH556 |
| B | HOH561 |
| B | HOH563 |
| B | HOH571 |
| B | HOH580 |
| B | HOH582 |
| B | HOH583 |
| B | HOH590 |
| B | HOH608 |
| B | HOH609 |
| B | HOH628 |
| B | HOH714 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| A | TYR278 |
| B | ALA395 |
| B | HOH546 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 403 |
| Chain | Residue |
| B | ARG44 |
| B | ALA45 |
| B | GLN102 |
| B | THR103 |
| B | ARG214 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | LEU301 |
| B | ARG335 |
| B | GLY339 |
| B | LEU389 |
| B | HOH644 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue FMT B 405 |
| Chain | Residue |
| B | ALA377 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 406 |
| Chain | Residue |
| B | ARG341 |
| B | PHE345 |
| site_id | AC9 |
| Number of Residues | 39 |
| Details | binding site for residue FAD C 401 |
| Chain | Residue |
| C | GLU32 |
| C | ARG33 |
| C | GLN34 |
| C | ARG42 |
| C | ARG44 |
| C | ALA45 |
| C | GLN102 |
| C | VAL127 |
| C | CYS158 |
| C | ASP159 |
| C | GLY160 |
| C | ILE164 |
| C | TYR222 |
| C | GLY285 |
| C | ASP286 |
| C | PRO293 |
| C | GLY298 |
| C | LEU299 |
| C | HOH535 |
| C | HOH538 |
| C | HOH542 |
| C | HOH548 |
| C | HOH550 |
| C | HOH551 |
| C | HOH553 |
| C | HOH564 |
| C | HOH573 |
| C | HOH584 |
| C | HOH593 |
| C | HOH601 |
| C | HOH604 |
| C | HOH610 |
| C | HOH648 |
| C | HOH682 |
| C | ILE8 |
| C | GLY9 |
| C | GLY11 |
| C | PRO12 |
| C | SER13 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| C | LEU301 |
| C | ARG335 |
| C | GLY339 |
| C | LEU389 |
| C | HOH533 |
| C | HOH654 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 403 |
| Chain | Residue |
| C | ARG44 |
| C | ALA45 |
| C | GLN102 |
| C | THR103 |
| C | ARG214 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 404 |
| Chain | Residue |
| C | ARG341 |
| C | PHE345 |
| D | PHE372 |
| site_id | AD4 |
| Number of Residues | 36 |
| Details | binding site for residue FAD D 401 |
| Chain | Residue |
| D | ILE8 |
| D | GLY9 |
| D | GLY11 |
| D | PRO12 |
| D | SER13 |
| D | GLU32 |
| D | ARG33 |
| D | GLN34 |
| D | ARG42 |
| D | ARG44 |
| D | ALA45 |
| D | GLN102 |
| D | VAL127 |
| D | CYS158 |
| D | ASP159 |
| D | GLY160 |
| D | GLY163 |
| D | ILE164 |
| D | TYR222 |
| D | GLY285 |
| D | ASP286 |
| D | GLY298 |
| D | LEU299 |
| D | HOH509 |
| D | HOH520 |
| D | HOH534 |
| D | HOH552 |
| D | HOH554 |
| D | HOH557 |
| D | HOH565 |
| D | HOH568 |
| D | HOH575 |
| D | HOH577 |
| D | HOH578 |
| D | HOH583 |
| D | HOH621 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 402 |
| Chain | Residue |
| D | LYS297 |
| D | GLY339 |
| D | LEU389 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 403 |
| Chain | Residue |
| D | GLN50 |
| D | THR96 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue CL D 404 |
| Chain | Residue |
| D | ARG44 |
| D | ALA45 |
| D | GLY101 |
| D | GLN102 |
| D | THR103 |
| D | ARG214 |
