6A5Z
Crystal structure of human FXR/RXR-LBD heterodimer bound to HNC180 and 9cRA and SRC1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0004879 | molecular_function | nuclear receptor activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0032052 | molecular_function | bile acid binding |
A | 0038183 | biological_process | bile acid signaling pathway |
D | 0003677 | molecular_function | DNA binding |
D | 0003707 | molecular_function | nuclear steroid receptor activity |
D | 0005634 | cellular_component | nucleus |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0008270 | molecular_function | zinc ion binding |
H | 0003677 | molecular_function | DNA binding |
H | 0004879 | molecular_function | nuclear receptor activity |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0032052 | molecular_function | bile acid binding |
H | 0038183 | biological_process | bile acid signaling pathway |
L | 0003677 | molecular_function | DNA binding |
L | 0003707 | molecular_function | nuclear steroid receptor activity |
L | 0005634 | cellular_component | nucleus |
L | 0006355 | biological_process | regulation of DNA-templated transcription |
L | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue 9R3 A 501 |
Chain | Residue |
A | MET290 |
A | TRP454 |
A | PHE461 |
A | MET328 |
A | PHE329 |
A | ARG331 |
A | SER332 |
A | ILE335 |
A | TYR369 |
A | HIS447 |
A | MET450 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue 9CR D 501 |
Chain | Residue |
D | ILE268 |
D | ALA271 |
D | ALA272 |
D | PHE313 |
D | ARG316 |
D | LEU326 |
D | ALA327 |
D | CYS432 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue 9R3 H 501 |
Chain | Residue |
H | MET265 |
H | MET290 |
H | MET328 |
H | PHE329 |
H | SER332 |
H | ILE335 |
H | LEU348 |
H | TYR369 |
H | HIS447 |
H | TRP454 |
H | PHE461 |
H | LEU465 |
H | TRP469 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue 9CR L 501 |
Chain | Residue |
L | ILE268 |
L | ALA271 |
L | ALA272 |
L | GLN275 |
L | PHE313 |
L | ARG316 |
L | LEU326 |
L | ALA327 |
L | ILE345 |
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 |
E | SER757 | |
F | SER641 | |
G | SER757 | |
I | SER641 | |
H | ARG331 | |
H | TYR361 | |
H | TYR369 | |
H | HIS447 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
D | SER259 | |
L | 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 |
D | SER260 | |
L | SER260 | |
H | LYS275 |