5TBP
Crystal Structure of RXR-alpha ligand binding domain complexed with synthetic modulator K8003
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 | 0003707 | molecular_function | nuclear steroid receptor activity |
B | 0005634 | cellular_component | nucleus |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0008270 | molecular_function | zinc ion binding |
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 | 0003707 | molecular_function | nuclear steroid receptor activity |
D | 0005634 | cellular_component | nucleus |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue 7A4 A 501 |
Chain | Residue |
A | ALA272 |
A | GLN275 |
A | LEU276 |
A | LEU301 |
A | ARG302 |
A | TRP305 |
C | PHE439 |
C | LYS440 |
C | LEU451 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue 7A4 A 502 |
Chain | Residue |
A | ILE268 |
A | ALA271 |
A | ALA272 |
A | GLN275 |
A | LEU309 |
A | PHE313 |
A | ARG316 |
A | ALA327 |
A | THR328 |
A | PHE438 |
A | ILE442 |
C | GOL501 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue 7A4 A 503 |
Chain | Residue |
A | VAL265 |
A | LEU436 |
A | PHE439 |
A | ILE447 |
C | ASP273 |
C | LEU276 |
C | ARG302 |
C | TRP305 |
C | GOL501 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue ACT A 504 |
Chain | Residue |
A | ARG285 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue ACT A 505 |
Chain | Residue |
A | HIS288 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue DMS A 506 |
Chain | Residue |
A | PRO287 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue ACT A 507 |
Chain | Residue |
A | PRO378 |
A | GLU390 |
A | ARG393 |
A | HOH602 |
B | LEU420 |
B | ARG421 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue ACT A 508 |
Chain | Residue |
A | LYS440 |
A | LEU441 |
A | ILE442 |
A | ASP444 |
A | THR445 |
A | PRO446 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue 7A4 B 501 |
Chain | Residue |
B | ASP273 |
B | LEU276 |
B | ARG302 |
B | TRP305 |
B | GOL502 |
D | VAL265 |
D | LEU436 |
D | PHE439 |
D | ILE447 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | PHE439 |
B | 7A4501 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue ACT B 503 |
Chain | Residue |
B | ARG234 |
B | ARG285 |
D | GLN460 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue ACT B 504 |
Chain | Residue |
B | GLN275 |
B | LEU309 |
B | PHE313 |
B | ARG316 |
B | LEU326 |
B | ALA327 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
A | 7A4502 |
A | 7A4503 |
C | PHE439 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue 7A4 D 501 |
Chain | Residue |
B | PHE439 |
B | LYS440 |
B | LEU451 |
D | ALA272 |
D | LEU276 |
D | LEU301 |
D | ARG302 |
D | TRP305 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue 7A4 D 502 |
Chain | Residue |
D | ALA271 |
D | ALA272 |
D | GLN275 |
D | LEU309 |
D | ARG316 |
D | ALA327 |
D | PHE438 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue ACT D 503 |
Chain | Residue |
D | ASP359 |
D | MET360 |
D | GLN361 |
D | GLN411 |
D | ARG414 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
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 | |
B | ARG316 | |
B | ALA327 | |
C | ARG316 | |
C | ALA327 | |
D | ARG316 | |
D | ALA327 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER259 | |
B | SER259 | |
C | SER259 | |
D | SER259 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700 |
Chain | Residue | Details |
A | SER260 | |
B | SER260 | |
C | SER260 | |
D | SER260 |