1XVP
crystal structure of CAR/RXR heterodimer bound with SRC1 peptide, fatty acid and CITCO
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 | 9 |
Details | BINDING SITE FOR RESIDUE F15 C 1001 |
Chain | Residue |
C | ILE268 |
C | ALA272 |
C | GLN275 |
C | PHE313 |
C | ARG316 |
C | LEU326 |
C | ALA327 |
C | ILE345 |
C | CYS432 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE F15 A 1002 |
Chain | Residue |
A | ALA272 |
A | GLN275 |
A | PHE313 |
A | ARG316 |
A | ALA327 |
A | ILE345 |
A | CYS432 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CID D 1003 |
Chain | Residue |
D | PHE161 |
D | ASN165 |
D | MET168 |
D | VAL199 |
D | HIS203 |
D | LEU206 |
D | PHE217 |
D | TYR224 |
D | THR225 |
D | ASP228 |
D | GLY229 |
D | LEU239 |
D | LEU242 |
D | PHE243 |
D | TYR326 |
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 | |
A | ALA327 | |
C | ARG316 | |
C | 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 |