1KKQ
Crystal structure of the human PPAR-alpha ligand-binding domain in complex with an antagonist GW6471 and a SMRT corepressor motif
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004879 | molecular_function | nuclear receptor activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004879 | molecular_function | nuclear receptor activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004879 | molecular_function | nuclear receptor activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| 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 | 15 |
| Details | BINDING SITE FOR RESIDUE 471 A 775 |
| Chain | Residue |
| A | LEU254 |
| A | PHE351 |
| A | ILE354 |
| A | HIS440 |
| A | VAL444 |
| A | LEU456 |
| A | HOH798 |
| A | GLU269 |
| A | ILE272 |
| A | PHE273 |
| A | CYS275 |
| A | CYS276 |
| A | SER280 |
| A | TYR314 |
| A | VAL332 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 471 B 776 |
| Chain | Residue |
| B | LEU254 |
| B | ILE272 |
| B | CYS276 |
| B | THR279 |
| B | SER280 |
| B | TYR314 |
| B | MET330 |
| B | VAL332 |
| B | LEU344 |
| B | PHE351 |
| B | ILE354 |
| B | MET355 |
| B | HIS440 |
| B | HOH794 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 471 C 777 |
| Chain | Residue |
| C | ILE241 |
| C | ILE272 |
| C | PHE273 |
| C | CYS275 |
| C | CYS276 |
| C | GLN277 |
| C | THR279 |
| C | SER280 |
| C | TYR314 |
| C | MET330 |
| C | VAL332 |
| C | PHE351 |
| C | ILE354 |
| C | HIS440 |
| C | HOH816 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 471 D 778 |
| Chain | Residue |
| D | LEU254 |
| D | GLU269 |
| D | ILE272 |
| D | PHE273 |
| D | CYS276 |
| D | GLN277 |
| D | SER280 |
| D | TYR314 |
| D | MET330 |
| D | VAL332 |
| D | LEU344 |
| D | PHE351 |
| D | HOH779 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19116277, ECO:0007744|PDB:3ET1 |
| Chain | Residue | Details |
| A | SER280 | |
| A | TYR314 | |
| A | TYR464 | |
| B | SER280 | |
| B | TYR314 | |
| B | TYR464 | |
| C | SER280 | |
| C | TYR314 | |
| C | TYR464 | |
| D | SER280 | |
| D | TYR314 | |
| D | TYR464 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Essential for heterodimerization with RXRA |
| Chain | Residue | Details |
| A | LEU433 | |
| B | LEU433 | |
| C | LEU433 | |
| D | LEU433 |
