2F0X
Crystal structure and function of human thioesterase superfamily member 2(THEM2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0005515 | molecular_function | protein binding |
| 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 | 0046872 | molecular_function | metal ion binding |
| 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 |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0005819 | cellular_component | spindle |
| C | 0005829 | cellular_component | cytosol |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0005819 | cellular_component | spindle |
| D | 0005829 | cellular_component | cytosol |
| D | 0005856 | cellular_component | cytoskeleton |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
| E | 0005515 | molecular_function | protein binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005759 | cellular_component | mitochondrial matrix |
| E | 0005819 | cellular_component | spindle |
| E | 0005829 | cellular_component | cytosol |
| E | 0005856 | cellular_component | cytoskeleton |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| E | 0051289 | biological_process | protein homotetramerization |
| E | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
| F | 0005515 | molecular_function | protein binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005759 | cellular_component | mitochondrial matrix |
| F | 0005819 | cellular_component | spindle |
| F | 0005829 | cellular_component | cytosol |
| F | 0005856 | cellular_component | cytoskeleton |
| F | 0006629 | biological_process | lipid metabolic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| F | 0051289 | biological_process | protein homotetramerization |
| F | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
| G | 0005515 | molecular_function | protein binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005739 | cellular_component | mitochondrion |
| G | 0005759 | cellular_component | mitochondrial matrix |
| G | 0005819 | cellular_component | spindle |
| G | 0005829 | cellular_component | cytosol |
| G | 0005856 | cellular_component | cytoskeleton |
| G | 0006629 | biological_process | lipid metabolic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| G | 0051289 | biological_process | protein homotetramerization |
| G | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
| H | 0005515 | molecular_function | protein binding |
| H | 0005634 | cellular_component | nucleus |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005739 | cellular_component | mitochondrion |
| H | 0005759 | cellular_component | mitochondrial matrix |
| H | 0005819 | cellular_component | spindle |
| H | 0005829 | cellular_component | cytosol |
| H | 0005856 | cellular_component | cytoskeleton |
| H | 0006629 | biological_process | lipid metabolic process |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| H | 0051289 | biological_process | protein homotetramerization |
| H | 0120163 | biological_process | negative regulation of cold-induced thermogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1001 |
| Chain | Residue |
| C | ASP65 |
| C | VAL82 |
| C | SER83 |
| C | HOH1031 |
| C | HOH1044 |
| D | ASN50 |
| D | LEU55 |
| D | HIS56 |
| D | GLY57 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | ASP65 |
| A | SER83 |
| A | HOH1064 |
| B | ASN50 |
| B | GLY57 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1003 |
| Chain | Residue |
| A | ARG23 |
| B | ARG23 |
| B | HOH1029 |
| B | HOH1039 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 H 1004 |
| Chain | Residue |
| G | ASN50 |
| G | GLY57 |
| H | ASP65 |
| H | SER83 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 F 1005 |
| Chain | Residue |
| E | ASN50 |
| E | LEU55 |
| E | GLY57 |
| F | ASP65 |
| F | VAL82 |
| F | SER83 |
| F | HOH1042 |
| F | HOH1069 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 G 1006 |
| Chain | Residue |
| G | ASP65 |
| G | SER83 |
| H | ASN50 |
| H | GLY57 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1007 |
| Chain | Residue |
| B | GLY110 |
| B | LYS111 |
| B | THR112 |
| B | LEU113 |
| D | HIS137 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1008 |
| Chain | Residue |
| A | ASN50 |
| A | GLY57 |
| B | ASP65 |
| B | SER83 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1009 |
| Chain | Residue |
| C | LYS37 |
| C | HIS105 |
| G | SER3 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 G 1010 |
| Chain | Residue |
| G | LYS111 |
| G | THR112 |
| G | LEU113 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1011 |
| Chain | Residue |
| A | GLY110 |
| A | LYS111 |
| A | THR112 |
| A | LEU113 |
| A | HOH1052 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1012 |
| Chain | Residue |
| B | HOH1023 |
| C | GLY110 |
| C | LYS111 |
| C | THR112 |
| C | LEU113 |
| C | HOH1071 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 H 1013 |
| Chain | Residue |
| F | HIS137 |
| H | GLY110 |
| H | LYS111 |
| H | THR112 |
| H | LEU113 |
| H | HOH1014 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 F 1014 |
| Chain | Residue |
| F | GLY110 |
| F | LYS111 |
| F | THR112 |
| F | LEU113 |
| F | HOH1045 |
| F | HOH1075 |
| H | HIS137 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1015 |
| Chain | Residue |
| D | GLY110 |
| D | LYS111 |
| D | THR112 |
| D | LEU113 |
| D | HOH1055 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1016 |
| Chain | Residue |
| C | ARG23 |
| D | ARG23 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1017 |
| Chain | Residue |
| E | ARG23 |
| E | HOH1055 |
| F | ARG23 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1018 |
| Chain | Residue |
| E | GLY110 |
| E | LYS111 |
| E | THR112 |
| E | LEU113 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1019 |
| Chain | Residue |
| E | ASP65 |
| E | SER83 |
| F | ASN50 |
| F | GLY57 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1020 |
| Chain | Residue |
| C | ASN50 |
| C | GLY57 |
| D | ASP65 |
| D | SER83 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19170545, ECO:0007744|PDB:3F5O |
| Chain | Residue | Details |
| A | GLU46 | |
| B | HIS137 | |
| C | GLU46 | |
| C | SER83 | |
| C | TYR90 | |
| C | LYS108 | |
| C | HIS137 | |
| D | GLU46 | |
| D | SER83 | |
| D | TYR90 | |
| D | LYS108 | |
| A | SER83 | |
| D | HIS137 | |
| E | GLU46 | |
| E | SER83 | |
| E | TYR90 | |
| E | LYS108 | |
| E | HIS137 | |
| F | GLU46 | |
| F | SER83 | |
| F | TYR90 | |
| F | LYS108 | |
| A | TYR90 | |
| F | HIS137 | |
| G | GLU46 | |
| G | SER83 | |
| G | TYR90 | |
| G | LYS108 | |
| G | HIS137 | |
| H | GLU46 | |
| H | SER83 | |
| H | TYR90 | |
| H | LYS108 | |
| A | LYS108 | |
| H | HIS137 | |
| A | HIS137 | |
| B | GLU46 | |
| B | SER83 | |
| B | TYR90 | |
| B | LYS108 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19170545, ECO:0007744|PDB:3F5O |
| Chain | Residue | Details |
| A | ASN50 | |
| E | GLY81 | |
| F | ASN50 | |
| F | GLY81 | |
| G | ASN50 | |
| G | GLY81 | |
| H | ASN50 | |
| H | GLY81 | |
| A | GLY81 | |
| B | ASN50 | |
| B | GLY81 | |
| C | ASN50 | |
| C | GLY81 | |
| D | ASN50 | |
| D | GLY81 | |
| E | ASN50 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
| Chain | Residue | Details |
| A | MSE1 | |
| B | MSE1 | |
| C | MSE1 | |
| D | MSE1 | |
| E | MSE1 | |
| F | MSE1 | |
| G | MSE1 | |
| H | MSE1 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 |
| Chain | Residue | Details |
| A | THR2 | |
| B | THR2 | |
| C | THR2 | |
| D | THR2 | |
| E | THR2 | |
| F | THR2 | |
| G | THR2 | |
| H | THR2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQR4 |
| Chain | Residue | Details |
| A | LYS27 | |
| B | LYS127 | |
| C | LYS27 | |
| C | LYS37 | |
| C | LYS43 | |
| C | LYS108 | |
| C | LYS127 | |
| D | LYS27 | |
| D | LYS37 | |
| D | LYS43 | |
| D | LYS108 | |
| A | LYS37 | |
| D | LYS127 | |
| E | LYS27 | |
| E | LYS37 | |
| E | LYS43 | |
| E | LYS108 | |
| E | LYS127 | |
| F | LYS27 | |
| F | LYS37 | |
| F | LYS43 | |
| F | LYS108 | |
| A | LYS43 | |
| F | LYS127 | |
| G | LYS27 | |
| G | LYS37 | |
| G | LYS43 | |
| G | LYS108 | |
| G | LYS127 | |
| H | LYS27 | |
| H | LYS37 | |
| H | LYS43 | |
| H | LYS108 | |
| A | LYS108 | |
| H | LYS127 | |
| A | LYS127 | |
| B | LYS27 | |
| B | LYS37 | |
| B | LYS43 | |
| B | LYS108 |
