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 |