4YFB
Structure of N-acylhomoserine lactone acylase MacQ in complex with phenylacetic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0017000 | biological_process | antibiotic biosynthetic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| G | 0017000 | biological_process | antibiotic biosynthetic process |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0017000 | biological_process | antibiotic biosynthetic process |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| J | 0017000 | biological_process | antibiotic biosynthetic process |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PAC C 601 |
| Chain | Residue |
| C | SER1 |
| C | THR69 |
| C | VAL70 |
| C | TRP165 |
| C | TRP189 |
| C | VAL190 |
| C | HOH1017 |
| C | PRO22 |
| C | HIS23 |
| C | TRP24 |
| C | PHE32 |
| C | PHE50 |
| C | GLN57 |
| C | ILE58 |
| C | HIS68 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 602 |
| Chain | Residue |
| C | ASP399 |
| C | LEU461 |
| C | CYS476 |
| C | THR485 |
| C | CYS486 |
| C | SER487 |
| C | TYR496 |
| C | HOH861 |
| C | HOH1058 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue PAC F 601 |
| Chain | Residue |
| F | SER1 |
| F | PRO22 |
| F | HIS23 |
| F | TRP24 |
| F | PHE32 |
| F | PHE50 |
| F | GLN57 |
| F | ILE58 |
| F | HIS68 |
| F | THR69 |
| F | VAL70 |
| F | TRP165 |
| F | TRP189 |
| F | VAL190 |
| F | HOH1019 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL F 602 |
| Chain | Residue |
| F | ASP399 |
| F | LEU461 |
| F | CYS476 |
| F | THR485 |
| F | CYS486 |
| F | SER487 |
| F | TYR496 |
| F | HOH794 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue PAC I 601 |
| Chain | Residue |
| I | SER1 |
| I | PRO22 |
| I | HIS23 |
| I | TRP24 |
| I | PHE32 |
| I | PHE50 |
| I | GLN57 |
| I | HIS68 |
| I | THR69 |
| I | VAL70 |
| I | TRP189 |
| I | VAL190 |
| I | HOH940 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL I 602 |
| Chain | Residue |
| I | ASP399 |
| I | LEU461 |
| I | CYS476 |
| I | MET479 |
| I | THR485 |
| I | CYS486 |
| I | SER487 |
| I | TYR496 |
| I | HOH760 |
| I | HOH865 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue PAC L 601 |
| Chain | Residue |
| L | SER1 |
| L | PRO22 |
| L | HIS23 |
| L | TRP24 |
| L | PHE32 |
| L | PHE50 |
| L | GLN57 |
| L | ILE58 |
| L | HIS68 |
| L | THR69 |
| L | VAL70 |
| L | TRP165 |
| L | TRP189 |
| L | VAL190 |
| L | HOH1044 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue GOL L 602 |
| Chain | Residue |
| L | ASP399 |
| L | LEU461 |
| L | CYS476 |
| L | MET479 |
| L | THR485 |
| L | CYS486 |
| L | SER487 |
| L | TYR496 |
| L | HOH835 |
| L | HOH1146 |
