1FM6
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 ROSIGLITAZONE 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 |
U | 0003677 | molecular_function | DNA binding |
U | 0003707 | molecular_function | nuclear steroid receptor activity |
U | 0005634 | cellular_component | nucleus |
U | 0006355 | biological_process | regulation of DNA-templated transcription |
U | 0008270 | molecular_function | zinc ion binding |
X | 0003677 | molecular_function | DNA binding |
X | 0004879 | molecular_function | nuclear receptor activity |
X | 0005634 | cellular_component | nucleus |
X | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 9CR A 501 |
Chain | Residue |
A | ALA271 |
A | GLN275 |
A | TRP305 |
A | PHE313 |
A | ARG316 |
A | LEU326 |
A | ALA327 |
A | CYS432 |
A | HIS435 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 9CR U 502 |
Chain | Residue |
U | ALA271 |
U | PHE313 |
U | ARG316 |
U | LEU326 |
U | ALA327 |
U | CYS432 |
U | HIS435 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BRL D 503 |
Chain | Residue |
D | ILE281 |
D | PHE282 |
D | GLY284 |
D | CYS285 |
D | SER289 |
D | HIS323 |
D | LEU330 |
D | ILE341 |
D | MET348 |
D | MET364 |
D | HIS449 |
D | LEU453 |
D | LEU469 |
D | TYR473 |
D | HOH583 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE BRL X 504 |
Chain | Residue |
X | PHE282 |
X | GLY284 |
X | CYS285 |
X | SER289 |
X | HIS323 |
X | TYR327 |
X | MET364 |
X | HIS449 |
X | LEU453 |
X | TYR473 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER641 | |
V | SER641 | |
E | SER698 | |
Y | SER698 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649 |
Chain | Residue | Details |
D | SER254 | |
U | SER259 | |
X | SER254 |
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 | |
U | SER260 |