1W8D
Binary structure of human DECR.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070402 | molecular_function | NADPH binding |
| A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| A | 1902494 | cellular_component | catalytic complex |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070402 | molecular_function | NADPH binding |
| B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| B | 1902494 | cellular_component | catalytic complex |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0005829 | cellular_component | cytosol |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0070402 | molecular_function | NADPH binding |
| C | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| C | 1902494 | cellular_component | catalytic complex |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0005829 | cellular_component | cytosol |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0006635 | biological_process | fatty acid beta-oxidation |
| D | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0070402 | molecular_function | NADPH binding |
| D | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| D | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP A1330 |
| Chain | Residue |
| A | GLY66 |
| A | VAL118 |
| A | ARG119 |
| A | ASN144 |
| A | ALA145 |
| A | ALA146 |
| A | ILE167 |
| A | ILE195 |
| A | THR196 |
| A | LYS214 |
| A | PRO240 |
| A | THR69 |
| A | GLY241 |
| A | PRO242 |
| A | ILE243 |
| A | THR245 |
| A | HOH2006 |
| A | HOH2048 |
| A | HOH2049 |
| A | GLY70 |
| A | LEU71 |
| A | SER90 |
| A | ARG91 |
| A | LYS92 |
| A | CYS116 |
| A | ASP117 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP B1330 |
| Chain | Residue |
| B | GLY66 |
| B | THR69 |
| B | GLY70 |
| B | LEU71 |
| B | SER90 |
| B | ARG91 |
| B | LYS92 |
| B | CYS116 |
| B | ASP117 |
| B | VAL118 |
| B | ARG119 |
| B | ASN144 |
| B | ALA145 |
| B | ALA146 |
| B | ILE167 |
| B | ILE195 |
| B | THR196 |
| B | LYS214 |
| B | ILE243 |
| B | HOH2006 |
| B | HOH2058 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP C1329 |
| Chain | Residue |
| C | GLY66 |
| C | THR69 |
| C | GLY70 |
| C | LEU71 |
| C | SER90 |
| C | ARG91 |
| C | LYS92 |
| C | CYS116 |
| C | ASP117 |
| C | VAL118 |
| C | ARG119 |
| C | ASN144 |
| C | ALA145 |
| C | ALA146 |
| C | ILE167 |
| C | ILE195 |
| C | THR196 |
| C | LYS214 |
| C | PRO240 |
| C | GLY241 |
| C | PRO242 |
| C | ILE243 |
| C | THR245 |
| C | HOH2003 |
| C | HOH2023 |
| C | HOH2049 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP D1329 |
| Chain | Residue |
| D | GLY66 |
| D | THR69 |
| D | GLY70 |
| D | LEU71 |
| D | SER90 |
| D | ARG91 |
| D | LYS92 |
| D | CYS116 |
| D | ASP117 |
| D | VAL118 |
| D | ASN144 |
| D | ALA145 |
| D | ALA146 |
| D | ILE195 |
| D | THR196 |
| D | LYS214 |
| D | PRO240 |
| D | GLY241 |
| D | PRO242 |
| D | ILE243 |
| D | THR245 |
| D | HOH2008 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A1329 |
| Chain | Residue |
| B | LEU47 |
| A | SER56 |
| A | LYS60 |
| A | SER286 |
| A | ASP287 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D1328 |
| Chain | Residue |
| C | MSE123 |
| C | ASN126 |
| D | GLN115 |
| D | ASP117 |
| D | MSE123 |
| D | HOH2061 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255 |
| Chain | Residue | Details |
| A | TYR199 | |
| B | TYR199 | |
| C | TYR199 | |
| D | TYR199 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15531764 |
| Chain | Residue | Details |
| A | GLY66 | |
| B | ARG119 | |
| B | PHE149 | |
| B | SER157 | |
| B | LYS214 | |
| B | PRO240 | |
| C | GLY66 | |
| C | ASP117 | |
| C | ARG119 | |
| C | PHE149 | |
| C | SER157 | |
| A | ASP117 | |
| C | LYS214 | |
| C | PRO240 | |
| D | GLY66 | |
| D | ASP117 | |
| D | ARG119 | |
| D | PHE149 | |
| D | SER157 | |
| D | LYS214 | |
| D | PRO240 | |
| A | ARG119 | |
| A | PHE149 | |
| A | SER157 | |
| A | LYS214 | |
| A | PRO240 | |
| B | GLY66 | |
| B | ASP117 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG91 | |
| A | ARG251 | |
| B | ARG91 | |
| B | ARG251 | |
| C | ARG91 | |
| C | ARG251 | |
| D | ARG91 | |
| D | ARG251 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ62 |
| Chain | Residue | Details |
| A | LYS42 | |
| B | LYS244 | |
| B | LYS260 | |
| B | LYS319 | |
| C | LYS42 | |
| C | LYS49 | |
| C | LYS97 | |
| C | LYS244 | |
| C | LYS260 | |
| C | LYS319 | |
| D | LYS42 | |
| A | LYS49 | |
| D | LYS49 | |
| D | LYS97 | |
| D | LYS244 | |
| D | LYS260 | |
| D | LYS319 | |
| A | LYS97 | |
| A | LYS244 | |
| A | LYS260 | |
| A | LYS319 | |
| B | LYS42 | |
| B | LYS49 | |
| B | LYS97 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR69 | |
| B | THR69 | |
| C | THR69 | |
| D | THR69 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CQ62 |
| Chain | Residue | Details |
| A | LYS73 | |
| B | LYS73 | |
| C | LYS73 | |
| D | LYS73 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS230 | |
| B | LYS230 | |
| C | LYS230 | |
| D | LYS230 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | VAL207 | |
| A | LYS214 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | VAL207 | |
| B | LYS214 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | VAL207 | |
| C | LYS214 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | VAL207 | |
| D | LYS214 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | LYS214 | |
| A | SER210 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | LYS214 | |
| B | SER210 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | LYS214 | |
| C | SER210 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | LYS214 | |
| D | SER210 |
