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. CrvCg.Dkasgf.HYnvlsCegCkgFFrR |
Chain | Residue | Details |
B | CYS87-ARG113 | |
A | CYS135-ARG161 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 154 |
Details | DNA_BIND: Nuclear receptor => ECO:0000255|PROSITE-ProRule:PRU00407 |
Chain | Residue | Details |
B | HIS84-SER161 | |
I | HIS84-SER161 |
site_id | SWS_FT_FI2 |
Number of Residues | 88 |
Details | ZN_FING: NR C4-type => ECO:0000255|PROSITE-ProRule:PRU00407 |
Chain | Residue | Details |
B | CYS87-CYS107 | |
B | CYS125-CYS149 | |
I | CYS87-CYS107 | |
I | CYS125-CYS149 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000269|PubMed:20159957 |
Chain | Residue | Details |
B | LYS410 | |
H | CYS138 | |
H | CYS152 | |
H | CYS155 | |
H | CYS171 | |
H | CYS177 | |
H | CYS187 | |
H | CYS190 | |
A | CYS138 | |
B | LYS448 | |
I | LYS410 | |
A | CYS171 | |
I | LYS448 | |
A | CYS187 | |
A | CYS190 | |
H | CYS135 |
site_id | SWS_FT_FI4 |
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 | |
H | ARG316 | |
H | ALA327 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER129 | |
H | SER129 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; by EP300 => ECO:0000269|PubMed:17761950 |
Chain | Residue | Details |
A | LYS145 | |
H | LYS145 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER259 | |
H | SER259 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700 |
Chain | Residue | Details |
A | SER260 | |
H | SER260 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:16912044 |
Chain | Residue | Details |
A | LYS108 | |
H | LYS108 |