7ON9
Crystal structure of para-hydroxybenzoate-3-hydroxylase PraI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| 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 | 0018671 | molecular_function | 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity |
| A | 0043639 | biological_process | benzoate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| A | 0106355 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADH) activity |
| A | 0106356 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADPH) activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| 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 | 0018671 | molecular_function | 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity |
| B | 0043639 | biological_process | benzoate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| B | 0106355 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADH) activity |
| B | 0106356 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADPH) activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| 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 | 0018671 | molecular_function | 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity |
| C | 0043639 | biological_process | benzoate catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| C | 0106355 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADH) activity |
| C | 0106356 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADPH) activity |
| D | 0004497 | molecular_function | monooxygenase activity |
| 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 | 0018671 | molecular_function | 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity |
| D | 0043639 | biological_process | benzoate catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
| D | 0106355 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADH) activity |
| D | 0106356 | molecular_function | 4-hydroxybenzoate 3-monooxygenase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE8 |
| A | ARG44 |
| A | ALA45 |
| A | GLY46 |
| A | VAL47 |
| A | GLN102 |
| A | VAL127 |
| A | CYS160 |
| A | ASP161 |
| A | GLY162 |
| A | PRO166 |
| A | GLY9 |
| A | VAL268 |
| A | GLY287 |
| A | ASP288 |
| A | PRO295 |
| A | ALA298 |
| A | LYS299 |
| A | GLY300 |
| A | LEU301 |
| A | ASN302 |
| A | PHB502 |
| A | GLY11 |
| A | HOH618 |
| A | HOH625 |
| A | HOH639 |
| A | HOH726 |
| A | HOH742 |
| A | HOH758 |
| A | HOH773 |
| A | HOH877 |
| A | PRO12 |
| A | ALA13 |
| A | ILE31 |
| A | GLU32 |
| A | ASN33 |
| A | ARG34 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue PHB A 502 |
| Chain | Residue |
| A | ARG44 |
| A | GLY46 |
| A | VAL47 |
| A | TYR203 |
| A | LEU212 |
| A | SER214 |
| A | ARG216 |
| A | TYR224 |
| A | PRO295 |
| A | THR296 |
| A | ALA298 |
| A | FAD501 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | ILE8 |
| B | GLY9 |
| B | GLY11 |
| B | PRO12 |
| B | ALA13 |
| B | ILE31 |
| B | GLU32 |
| B | ASN33 |
| B | ARG34 |
| B | ARG44 |
| B | ALA45 |
| B | GLY46 |
| B | VAL47 |
| B | GLN102 |
| B | VAL127 |
| B | CYS160 |
| B | ASP161 |
| B | GLY162 |
| B | PRO166 |
| B | VAL268 |
| B | GLY287 |
| B | ASP288 |
| B | ALA298 |
| B | LYS299 |
| B | GLY300 |
| B | LEU301 |
| B | ASN302 |
| B | HOH678 |
| B | HOH679 |
| B | HOH717 |
| B | HOH738 |
| B | HOH760 |
| B | HOH761 |
| B | HOH770 |
| B | HOH839 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue PHB B 502 |
| Chain | Residue |
| B | ARG44 |
| B | GLY46 |
| B | VAL47 |
| B | TYR203 |
| B | SER214 |
| B | ARG216 |
| B | TYR224 |
| B | PRO295 |
| B | THR296 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | GLU32 |
| C | ASN33 |
| C | ARG34 |
| C | ARG44 |
| C | ALA45 |
| C | VAL47 |
| C | GLN102 |
| C | VAL127 |
| C | CYS160 |
| C | ASP161 |
| C | GLY162 |
| C | PRO166 |
| C | GLY287 |
| C | ASP288 |
| C | ALA298 |
| C | LYS299 |
| C | GLY300 |
| C | LEU301 |
| C | ASN302 |
| C | HOH624 |
| C | HOH644 |
| C | HOH675 |
| C | HOH687 |
| C | HOH745 |
| C | HOH760 |
| C | HOH779 |
| C | ILE8 |
| C | GLY9 |
| C | GLY11 |
| C | PRO12 |
| C | ALA13 |
| C | ILE31 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue PHB C 502 |
| Chain | Residue |
| C | ALA45 |
| C | TYR203 |
| C | SER214 |
| C | ARG216 |
| C | ARG222 |
| C | TYR224 |
| C | PRO295 |
| C | THR296 |
| C | HOH730 |
| site_id | AC7 |
| Number of Residues | 34 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| D | ILE8 |
| D | GLY9 |
| D | GLY11 |
| D | PRO12 |
| D | ALA13 |
| D | ILE31 |
| D | GLU32 |
| D | ASN33 |
| D | ARG34 |
| D | ARG44 |
| D | ALA45 |
| D | VAL47 |
| D | GLN102 |
| D | VAL127 |
| D | CYS160 |
| D | ASP161 |
| D | GLY162 |
| D | PRO166 |
| D | GLY287 |
| D | ASP288 |
| D | PRO295 |
| D | ALA298 |
| D | LYS299 |
| D | GLY300 |
| D | LEU301 |
| D | ASN302 |
| D | HOH609 |
| D | HOH612 |
| D | HOH672 |
| D | HOH691 |
| D | HOH705 |
| D | HOH726 |
| D | HOH737 |
| D | HOH747 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue PHB D 502 |
| Chain | Residue |
| D | ALA45 |
| D | VAL47 |
| D | TYR203 |
| D | SER214 |
| D | ARG216 |
| D | ARG222 |
| D | TYR224 |
| D | PRO295 |
| D | THR296 |
| D | HOH660 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P20586","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P20586","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
