1XV9
crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid, and 5b-pregnane-3,20-dione.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003707 | molecular_function | nuclear steroid receptor activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004879 | molecular_function | nuclear receptor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003707 | molecular_function | nuclear steroid receptor activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0008270 | molecular_function | zinc ion binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0004879 | molecular_function | nuclear receptor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CI2 D 1001 |
| Chain | Residue |
| B | HIS160 |
| D | PHE161 |
| D | ILE164 |
| D | ASN165 |
| D | MET168 |
| D | HIS203 |
| D | TYR224 |
| D | LEU242 |
| D | TYR326 |
| B | PHE161 |
| B | ILE164 |
| B | ASN165 |
| B | HIS203 |
| B | TYR224 |
| B | PHE238 |
| B | LEU242 |
| B | TYR326 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F15 C 1002 |
| Chain | Residue |
| C | ALA272 |
| C | GLN275 |
| C | LEU309 |
| C | PHE313 |
| C | ARG316 |
| C | ALA327 |
| C | ILE345 |
| C | PHE346 |
| C | CYS432 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE F15 A 1003 |
| Chain | Residue |
| A | ILE268 |
| A | ALA272 |
| A | GLN275 |
| A | PHE313 |
| A | ARG316 |
| A | ALA327 |
| A | ILE345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL, ECO:0007744|PDB:3FC6 |
| Chain | Residue | Details |
| A | ARG316 | |
| C | ARG316 | |
| C | ALA327 | |
| A | ALA327 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER259 | |
| C | SER259 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700 |
| Chain | Residue | Details |
| A | SER260 | |
| C | SER260 |
