1MZN
CRYSTAL STRUCTURE at 1.9 ANGSTROEMS RESOLUTION OF THE HOMODIMER OF HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO THE SYNTHETIC AGONIST COMPOUND BMS 649 AND A COACTIVATOR PEPTIDE
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 |
| 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 |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003707 | molecular_function | nuclear steroid receptor activity |
| E | 0005634 | cellular_component | nucleus |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0008270 | molecular_function | zinc ion binding |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003707 | molecular_function | nuclear steroid receptor activity |
| G | 0005634 | cellular_component | nucleus |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BM6 A 200 |
| Chain | Residue |
| A | ILE268 |
| A | LEU326 |
| A | ALA327 |
| A | CYS432 |
| A | HIS435 |
| A | HOH4020 |
| A | ALA271 |
| A | ALA272 |
| A | GLN275 |
| A | ASN306 |
| A | LEU309 |
| A | ILE310 |
| A | PHE313 |
| A | ARG316 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BM6 C 1200 |
| Chain | Residue |
| C | ILE1268 |
| C | ALA1271 |
| C | ALA1272 |
| C | GLN1275 |
| C | ASN1306 |
| C | LEU1309 |
| C | ILE1310 |
| C | PHE1313 |
| C | ARG1316 |
| C | LEU1326 |
| C | ALA1327 |
| C | CYS1432 |
| C | HIS1435 |
| C | PHE1439 |
| C | HOH4076 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BM6 E 2200 |
| Chain | Residue |
| E | ILE2268 |
| E | ALA2271 |
| E | ALA2272 |
| E | GLN2275 |
| E | ASN2306 |
| E | LEU2309 |
| E | ILE2310 |
| E | PHE2313 |
| E | ARG2316 |
| E | LEU2326 |
| E | ALA2327 |
| E | CYS2432 |
| E | HIS2435 |
| E | HOH4010 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BM6 G 3200 |
| Chain | Residue |
| G | ILE3268 |
| G | ALA3271 |
| G | ALA3272 |
| G | GLN3275 |
| G | ASN3306 |
| G | LEU3309 |
| G | ILE3310 |
| G | PHE3313 |
| G | ARG3316 |
| G | LEU3326 |
| G | ALA3327 |
| G | CYS3432 |
| G | HIS3435 |
| G | HOH4057 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| 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 | |
| A | ALA327 | |
| C | ARG1316 | |
| C | ALA1327 | |
| E | ARG2316 | |
| E | ALA2327 | |
| G | ARG3316 | |
| G | ALA3327 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER259 | |
| C | SER1259 | |
| E | SER2259 | |
| G | SER3259 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700 |
| Chain | Residue | Details |
| A | SER260 | |
| C | SER1260 | |
| E | SER2260 | |
| G | SER3260 |
