4QD8
Crystal structure of Thioesterase PA1618 from Pseudomonas aeruginosa in complex with phenacyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 0FQ C 201 |
| Chain | Residue |
| C | HIS108 |
| E | HIS55 |
| E | GLY56 |
| E | HIS91 |
| E | LEU92 |
| E | ARG93 |
| E | GLY94 |
| E | LYS126 |
| F | GLU64 |
| F | SER68 |
| F | MET69 |
| C | GLY110 |
| F | GLY84 |
| F | LEU85 |
| C | ARG111 |
| C | THR112 |
| C | THR113 |
| C | HOH307 |
| C | HOH317 |
| E | GLN49 |
| E | PRO50 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 0FQ C 202 |
| Chain | Residue |
| C | GLN49 |
| C | PRO50 |
| C | HIS55 |
| C | GLY56 |
| C | HIS91 |
| C | LEU92 |
| C | ARG93 |
| C | ARG96 |
| C | HOH322 |
| D | GLU64 |
| D | SER68 |
| D | MET69 |
| D | GLY84 |
| D | LEU85 |
| E | HIS108 |
| E | GLY110 |
| E | ARG111 |
| E | THR112 |
| E | THR113 |
| E | HOH203 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE 0FQ D 201 |
| Chain | Residue |
| B | ARG28 |
| D | HIS108 |
| D | LEU109 |
| D | GLY110 |
| D | ARG111 |
| D | THR112 |
| D | THR113 |
| D | HOH311 |
| D | HOH331 |
| D | HOH384 |
| E | GLU64 |
| E | SER68 |
| E | GLY84 |
| E | LEU85 |
| F | GLN49 |
| F | PRO50 |
| F | LEU54 |
| F | HIS55 |
| F | GLY56 |
| F | HIS91 |
| F | LEU92 |
| F | ARG93 |
| F | GLY94 |
| F | HOH225 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE 0FQ D 202 |
| Chain | Residue |
| A | ARG28 |
| A | GLU30 |
| A | HOH267 |
| C | GLU64 |
| C | SER68 |
| C | GLY84 |
| C | LEU85 |
| C | HOH332 |
| D | GLN49 |
| D | PRO50 |
| D | LEU54 |
| D | HIS55 |
| D | GLY56 |
| D | HIS91 |
| D | LEU92 |
| D | ARG93 |
| D | GLY94 |
| D | PRO127 |
| D | HOH330 |
| F | HIS108 |
| F | GLY110 |
| F | ARG111 |
| F | THR112 |
| F | THR113 |
| F | HOH205 |






