2CY9
Crystal structure of thioesterase superfamily member2 from Mus musculus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005819 | cellular_component | spindle |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005819 | cellular_component | spindle |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9NPJ3 |
| Chain | Residue | Details |
| A | GLU46 | |
| B | GLY81 | |
| B | SER83 | |
| B | TYR90 | |
| B | LYS108 | |
| B | HIS137 | |
| A | ASN50 | |
| A | GLY81 | |
| A | SER83 | |
| A | TYR90 | |
| A | LYS108 | |
| A | HIS137 | |
| B | GLU46 | |
| B | ASN50 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q9NPJ3 |
| Chain | Residue | Details |
| A | MSE1 | |
| B | MSE1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753 |
| Chain | Residue | Details |
| A | LYS27 | |
| B | LYS127 | |
| A | LYS37 | |
| A | LYS43 | |
| A | LYS108 | |
| A | LYS127 | |
| B | LYS27 | |
| B | LYS37 | |
| B | LYS43 | |
| B | LYS108 |
