Crystal Structure of the ARNT PAS-B homodimer. Determined by X-ray diffraction at 1.6 Å resolution. Released 17 Apr 2013.
Explore 4EQ1 in 3D Show helices and sheets RCSB PDB PDBe
4EQ1 contains 13 α-helices and 18 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-360 | 2 | |
| β-strand | 362-367 | 6 | 2 |
| β-strand | 372 | 1 | 3 |
| β-strand | 373-376 | 4 | 2 |
| α-helix | 379-384 | 6 | |
| α-helix | 388-391 | 4 | |
| β-strand | 395 | 1 | 3 |
| α-helix | 396-399 | 4 | |
| β-strand | 400 | 1 | 2 |
| α-helix | 402-404 | 3 | |
| α-helix | 405-417 | 13 | |
| β-strand | 422-430 | 9 | 2 |
| β-strand | 436-447 | 12 | 2 |
| α-helix | 448 | 1 | |
| β-strand | 454-463 | 10 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 357-358 | 2 | 2 |
| β-strand | 362-367 | 6 | 1 |
| β-strand | 372 | 1 | 4 |
| β-strand | 373-376 | 4 | 1 |
| α-helix | 379-384 | 6 | |
| α-helix | 388-391 | 4 | |
| β-strand | 395 | 1 | 4 |
| α-helix | 396-399 | 4 | |
| β-strand | 400 | 1 | 1 |
| α-helix | 402-404 | 3 | |
| α-helix | 405-417 | 13 | |
| β-strand | 422-430 | 9 | 1 |
| β-strand | 436-447 | 12 | 1 |
| α-helix | 448 | 1 | |
| β-strand | 454-463 | 10 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aryl hydrocarbon receptor nuclear translocator | A, B | protein | 109 | Homo sapiens | P27540 (AlphaFold model) |
>4EQ1_1 Aryl hydrocarbon receptor nuclear translocator (chains A, B) GVCQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQV VKLKGQVLSVMFRFRSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNV
| ID | Name | Formula | Copies |
|---|---|---|---|
| PE5 | 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol | C18 H38 O9 | 1 |
Regulating the ARNT/TACC3 Axis: Multiple Approaches to Manipulating Protein/Protein Interactions with Small Molecules. Guo, Y., Partch, C.L., Key, J. et al. ACS Chem Biol (2013) 8:626-635. DOI 10.1021/cb300604u · PubMed
Other PDB entries of the same protein (UniProt P27540 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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