2QQ2
Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016790 | molecular_function | thiolester hydrolase activity |
| B | 0016790 | molecular_function | thiolester hydrolase activity |
| C | 0016790 | molecular_function | thiolester hydrolase activity |
| D | 0016790 | molecular_function | thiolester hydrolase activity |
| E | 0016790 | molecular_function | thiolester hydrolase activity |
| F | 0016790 | molecular_function | thiolester hydrolase activity |
| G | 0016790 | molecular_function | thiolester hydrolase activity |
| H | 0016790 | molecular_function | thiolester hydrolase activity |
| I | 0016790 | molecular_function | thiolester hydrolase activity |
| J | 0016790 | molecular_function | thiolester hydrolase activity |
| K | 0016790 | molecular_function | thiolester hydrolase activity |
| L | 0016790 | molecular_function | thiolester hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 456 |
| Details | Domain: {"description":"HotDog ACOT-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01106","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
