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 | |