Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004879 | molecular_function | nuclear receptor activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004879 | molecular_function | nuclear receptor activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0003677 | molecular_function | DNA binding |
| E | 0004879 | molecular_function | nuclear receptor activity |
| E | 0005634 | cellular_component | nucleus |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0003677 | molecular_function | DNA binding |
| G | 0004879 | molecular_function | nuclear receptor activity |
| G | 0005634 | cellular_component | nucleus |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE YT3 C 469 |
| Chain | Residue |
| A | GLU267 |
| A | GLU451 |
| A | ASP453 |
| C | GLU267 |
| C | GLU451 |
| C | ASP453 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE YT3 E 469 |
| Chain | Residue |
| G | GLU267 |
| G | GLU451 |
| G | ASP453 |
| E | GLU267 |
| E | GLU451 |
| E | ASP453 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 544 A 469 |
| Chain | Residue |
| A | PHE273 |
| A | CYS275 |
| A | CYS276 |
| A | SER280 |
| A | TYR314 |
| A | LEU321 |
| A | VAL332 |
| A | PHE351 |
| A | ILE354 |
| A | MET355 |
| A | HIS440 |
| A | TYR464 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 544 C 470 |
| Chain | Residue |
| C | LEU247 |
| C | GLU269 |
| C | PHE273 |
| C | CYS275 |
| C | CYS276 |
| C | GLN277 |
| C | SER280 |
| C | TYR314 |
| C | MET330 |
| C | VAL332 |
| C | LEU347 |
| C | PHE351 |
| C | ILE354 |
| C | HIS440 |
| C | VAL444 |
| C | TYR464 |
| C | HOH527 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 544 E 501 |
| Chain | Residue |
| E | GLU269 |
| E | PHE273 |
| E | CYS275 |
| E | CYS276 |
| E | SER280 |
| E | TYR314 |
| E | MET330 |
| E | VAL332 |
| E | PHE351 |
| E | ILE354 |
| E | MET355 |
| E | HIS440 |
| E | LEU460 |
| E | TYR464 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 544 G 601 |
| Chain | Residue |
| G | LEU247 |
| G | ILE272 |
| G | PHE273 |
| G | CYS275 |
| G | CYS276 |
| G | THR279 |
| G | SER280 |
| G | TYR314 |
| G | LEU321 |
| G | MET330 |
| G | VAL332 |
| G | LEU347 |
| G | PHE351 |
| G | ILE354 |
| G | MET355 |
| G | HIS440 |
| G | LEU460 |
| G | TYR464 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | SER698 | |
| G | SER280 | |
| G | TYR314 | |
| G | TYR464 | |
| D | SER698 | |
| F | SER698 | |
| H | SER698 | |
| C | TYR314 | |
| C | TYR464 | |
| E | SER280 | |
| E | TYR314 | |
| E | TYR464 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Essential for heterodimerization with RXRA |
| Chain | Residue | Details |
| A | LEU433 | |
| C | LEU433 | |
| E | LEU433 | |
| G | LEU433 | |
