5T07
Crystal structure of a putative acyl-CoA thioesterase EC709/ECK0725 from Escherichia coli in complex with Decanoyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016790 | molecular_function | thiolester hydrolase activity |
| A | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016790 | molecular_function | thiolester hydrolase activity |
| B | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016790 | molecular_function | thiolester hydrolase activity |
| C | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016790 | molecular_function | thiolester hydrolase activity |
| D | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue MFK A 201 |
| Chain | Residue |
| A | ALA19 |
| A | HOH314 |
| A | HOH315 |
| A | HOH335 |
| A | HOH379 |
| A | HOH392 |
| C | TYR14 |
| C | GLU53 |
| C | SER127 |
| C | HOH430 |
| D | ALA56 |
| A | GLY20 |
| D | PHE57 |
| D | VAL59 |
| D | ARG60 |
| D | PRO116 |
| D | MET119 |
| D | PRO121 |
| A | VAL23 |
| A | TYR24 |
| A | HIS25 |
| A | TYR66 |
| A | TYR67 |
| A | ALA68 |
| A | PRO69 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | binding site for residue MFK C 201 |
| Chain | Residue |
| B | ALA19 |
| B | GLY20 |
| B | VAL23 |
| B | TYR24 |
| B | HIS25 |
| B | TYR66 |
| B | TYR67 |
| B | ALA68 |
| B | PRO69 |
| B | HOH207 |
| B | HOH209 |
| C | MET51 |
| C | ALA56 |
| C | VAL58 |
| C | VAL59 |
| C | ARG60 |
| C | ARG86 |
| C | GLY87 |
| C | THR88 |
| C | SER89 |
| C | LEU110 |
| C | PRO116 |
| C | MET119 |
| C | HOH301 |
| C | HOH303 |
| C | HOH308 |
| C | HOH310 |
| C | HOH313 |
| C | HOH323 |
| D | TYR14 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue MFK D 201 |
| Chain | Residue |
| A | MET51 |
| A | PHE57 |
| A | VAL58 |
| A | VAL59 |
| A | ARG60 |
| A | MET119 |
| A | PRO121 |
| B | TYR14 |
| B | ALA52 |
| B | GLU53 |
| B | SER127 |
| B | HOH273 |
| D | ALA19 |
| D | VAL23 |
| D | TYR24 |
| D | HIS25 |
| D | TYR66 |
| D | TYR67 |
| D | ALA68 |
| D | PRO69 |
| D | THR102 |
| D | HOH301 |
| D | HOH307 |
| D | HOH325 |
| D | HOH335 |
| D | HOH350 |
| D | HOH354 |
| D | HOH357 |
| D | HOH367 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10041","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
