1FM9
THE 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE HETERODIMER OF THE HUMAN RXRALPHA AND PPARGAMMA LIGAND BINDING DOMAINS RESPECTIVELY BOUND WITH 9-CIS RETINOIC ACID AND GI262570 AND CO-ACTIVATOR PEPTIDES.
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 |
| D | 0003677 | molecular_function | DNA binding |
| D | 0004879 | molecular_function | nuclear receptor activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 570 D 200 |
| Chain | Residue |
| D | HOH63 |
| D | LEU330 |
| D | ILE341 |
| D | MET348 |
| D | PHE360 |
| D | MET364 |
| D | HIS449 |
| D | LEU465 |
| D | LEU469 |
| D | TYR473 |
| D | ARG280 |
| D | PHE282 |
| D | GLY284 |
| D | CYS285 |
| D | GLN286 |
| D | SER289 |
| D | HIS323 |
| D | TYR327 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 9CR A 201 |
| Chain | Residue |
| A | ALA271 |
| A | GLN275 |
| A | TRP305 |
| A | PHE313 |
| A | ARG316 |
| A | LEU326 |
| A | ALA327 |
| A | CYS432 |
| A | HIS435 |
| A | LEU436 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 496 |
| Details | Domain: {"description":"NR LBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01189","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Region: {"description":"Required for nuclear export","evidences":[{"source":"PubMed","id":"15509776","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16107141","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18800767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19167885","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ACL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FAL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FC6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by MAPK8 and MAPK9","evidences":[{"source":"UniProtKB","id":"P28700","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Motif: {"description":"9aaTAD","evidences":[{"source":"PubMed","id":"30468856","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9744270","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PRG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"36737649","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Motif: {"description":"LXXLL motif 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
