1BY4
STRUCTURE AND MECHANISM OF THE HOMODIMERIC ASSEMBLY OF THE RXR ON DNA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| 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 | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0043565 | molecular_function | sequence-specific DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1330 |
| Chain | Residue |
| A | CYS1135 |
| A | CYS1138 |
| A | CYS1152 |
| A | CYS1155 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1331 |
| Chain | Residue |
| A | CYS1171 |
| A | CYS1177 |
| A | CYS1187 |
| A | CYS1190 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1335 |
| Chain | Residue |
| B | CYS1238 |
| B | CYS1252 |
| B | CYS1255 |
| B | CYS1235 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1336 |
| Chain | Residue |
| B | CYS1271 |
| B | CYS1277 |
| B | CYS1287 |
| B | CYS1290 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 2330 |
| Chain | Residue |
| C | CYS2135 |
| C | CYS2138 |
| C | CYS2152 |
| C | CYS2155 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 2331 |
| Chain | Residue |
| C | CYS2171 |
| C | ASP2176 |
| C | CYS2177 |
| C | CYS2187 |
| C | CYS2190 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 2335 |
| Chain | Residue |
| D | CYS2235 |
| D | CYS2238 |
| D | CYS2252 |
| D | CYS2255 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 2336 |
| Chain | Residue |
| D | CYS2271 |
| D | CYS2277 |
| D | CYS2287 |
| D | CYS2290 |
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 | CYS1135-ARG1161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 260 |
| Details | DNA_BIND: Nuclear receptor => ECO:0000255|PROSITE-ProRule:PRU00407 |
| Chain | Residue | Details |
| A | CYS1135-MET1200 | |
| B | CYS1235-MET1300 | |
| C | CYS2135-MET2200 | |
| D | CYS2235-MET2300 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 176 |
| Details | ZN_FING: NR C4-type => ECO:0000255|PROSITE-ProRule:PRU00407 |
| Chain | Residue | Details |
| A | CYS1135-CYS1155 | |
| A | CYS1171-CYS1195 | |
| B | CYS1235-CYS1255 | |
| B | CYS1271-CYS1295 | |
| C | CYS2135-CYS2155 | |
| C | CYS2171-CYS2195 | |
| D | CYS2235-CYS2255 | |
| D | CYS2271-CYS2295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10669605, ECO:0007744|PDB:1BY4 |
| Chain | Residue | Details |
| A | CYS1135 | |
| B | CYS1238 | |
| B | CYS1252 | |
| B | CYS1255 | |
| B | CYS1271 | |
| B | CYS1277 | |
| B | CYS1287 | |
| B | CYS1290 | |
| C | CYS2135 | |
| C | CYS2138 | |
| C | CYS2152 | |
| A | CYS1138 | |
| C | CYS2155 | |
| C | CYS2171 | |
| C | CYS2177 | |
| C | CYS2187 | |
| C | CYS2190 | |
| D | CYS2235 | |
| D | CYS2238 | |
| D | CYS2252 | |
| D | CYS2255 | |
| D | CYS2271 | |
| A | CYS1152 | |
| D | CYS2277 | |
| D | CYS2287 | |
| D | CYS2290 | |
| A | CYS1155 | |
| A | CYS1171 | |
| A | CYS1177 | |
| A | CYS1187 | |
| A | CYS1190 | |
| B | CYS1235 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER1129 | |
| B | SER1229 | |
| C | SER2129 | |
| D | SER2229 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; by EP300 => ECO:0000269|PubMed:17761950 |
| Chain | Residue | Details |
| A | LYS1145 | |
| B | LYS1245 | |
| C | LYS2145 | |
| D | LYS2245 |
