4NQA
Crystal structure of liganded hRXR-alpha/hLXR-beta heterodimer on DNA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| 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 |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0004879 | molecular_function | nuclear receptor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003700 | molecular_function | DNA-binding transcription factor activity |
| H | 0003707 | molecular_function | nuclear steroid receptor activity |
| H | 0005634 | cellular_component | nucleus |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0008270 | molecular_function | zinc ion binding |
| H | 0043565 | molecular_function | sequence-specific DNA binding |
| I | 0003677 | molecular_function | DNA binding |
| I | 0003700 | molecular_function | DNA-binding transcription factor activity |
| I | 0004879 | molecular_function | nuclear receptor activity |
| I | 0006355 | biological_process | regulation of DNA-templated transcription |
| I | 0006629 | biological_process | lipid metabolic process |
| I | 0008270 | molecular_function | zinc ion binding |
| I | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 9CR A 501 |
| Chain | Residue |
| A | ILE268 |
| A | GLN275 |
| A | PHE313 |
| A | ARG316 |
| A | ALA327 |
| A | CYS432 |
| A | HIS435 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | CYS152 |
| A | CYS155 |
| A | ARG184 |
| A | CYS135 |
| A | CYS138 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 503 |
| Chain | Residue |
| A | CYS171 |
| A | CYS177 |
| A | CYS187 |
| A | CYS190 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 965 B 501 |
| Chain | Residue |
| B | PHE271 |
| B | LEU274 |
| B | ALA275 |
| B | SER278 |
| B | ILE309 |
| B | MET312 |
| B | LEU313 |
| B | THR316 |
| B | ARG319 |
| B | PHE329 |
| B | LEU330 |
| B | PHE340 |
| B | PHE354 |
| B | HIS435 |
| B | TRP457 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | CYS87 |
| B | CYS90 |
| B | CYS104 |
| B | CYS107 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 503 |
| Chain | Residue |
| B | CYS125 |
| B | CYS131 |
| B | CYS141 |
| B | CYS144 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 9CR H 501 |
| Chain | Residue |
| H | ALA271 |
| H | GLN275 |
| H | PHE313 |
| H | ARG316 |
| H | LEU326 |
| H | ALA327 |
| H | ILE345 |
| H | CYS432 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 502 |
| Chain | Residue |
| H | CYS135 |
| H | CYS138 |
| H | CYS152 |
| H | CYS155 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 503 |
| Chain | Residue |
| H | CYS171 |
| H | CYS177 |
| H | CYS187 |
| H | CYS190 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 965 I 501 |
| Chain | Residue |
| I | PHE271 |
| I | LEU274 |
| I | ALA275 |
| I | SER278 |
| I | GLU281 |
| I | MET312 |
| I | LEU313 |
| I | THR316 |
| I | ARG319 |
| I | PHE329 |
| I | LEU330 |
| I | PHE340 |
| I | LEU345 |
| I | PHE349 |
| I | ILE350 |
| I | ILE353 |
| I | PHE354 |
| I | HIS435 |
| I | TRP457 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN I 502 |
| Chain | Residue |
| I | CYS87 |
| I | CYS90 |
| I | CYS104 |
| I | CYS107 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN I 503 |
| Chain | Residue |
| I | CYS125 |
| I | CYS131 |
| I | CYS141 |
| I | CYS144 |
Functional Information from PROSITE/UniProt
| site_id | PS00031 |
| Number of Residues | 27 |
| Details | NUCLEAR_REC_DBD_1 Nuclear hormones receptors DNA-binding region signature. CaiCg.Drssgk.HYgvysCegCkgFFkR |
| Chain | Residue | Details |
| A | CYS135-ARG161 | |
| B | CYS87-ARG113 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 284 |
| Details | DNA binding: {"description":"Nuclear receptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00407","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 176 |
| Details | Zinc finger: {"description":"NR C4-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00407","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Region: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"12145331","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Region: {"description":"Required for nuclear export","evidences":[{"source":"PubMed","id":"15509776","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10669605","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BY4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| 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_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; by EP300","evidences":[{"source":"PubMed","id":"17761950","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| 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_FI11 |
| Number of Residues | 23 |
| Details | Region: {"description":"Hinge"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 70 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 12 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 16 |
| Details | Compositional bias: {"description":"Gly residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"20159957","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 16 |
| Details | Motif: {"description":"LXXLL motif 2"} |
| Chain | Residue | Details |






