Crystal structure of a high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains. Determined by X-ray diffraction at 1.17 Å resolution. Released 20 Jan 2009.
Explore 3F1P in 3D Show helices and sheets RCSB PDB PDBe
3F1P contains 12 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 |
|---|---|---|---|
| α-helix | 240-242 | 3 | |
| β-strand | 243-248 | 6 | 1 |
| β-strand | 253 | 1 | 2 |
| β-strand | 254-257 | 4 | 1 |
| α-helix | 260-265 | 6 | |
| α-helix | 269-272 | 4 | |
| β-strand | 276 | 1 | 2 |
| α-helix | 277-280 | 4 | |
| β-strand | 281 | 1 | 1 |
| α-helix | 283-285 | 3 | |
| α-helix | 286-299 | 14 | |
| β-strand | 301-303 | 3 | 1 |
| β-strand | 307-310 | 4 | 1 |
| β-strand | 316-328 | 13 | 1 |
| β-strand | 333-343 | 11 | 1 |
| β-strand | 348 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 359-361 | 3 | |
| β-strand | 362-367 | 6 | 3 |
| β-strand | 372 | 1 | 4 |
| β-strand | 373-376 | 4 | 3 |
| α-helix | 380-384 | 5 | |
| α-helix | 388-390 | 3 | |
| β-strand | 395 | 1 | 4 |
| α-helix | 396-399 | 4 | |
| β-strand | 400 | 1 | 3 |
| α-helix | 405-415 | 11 | |
| β-strand | 423-430 | 8 | 3 |
| β-strand | 436-446 | 11 | 3 |
| α-helix | 453-455 | 3 | |
| β-strand | 456-463 | 8 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endothelial PAS domain-containing protein 1 | A | protein | 117 | Homo sapiens | Q99814 (AlphaFold model) |
| Aryl hydrocarbon receptor nuclear translocator | B | protein | 121 | Homo sapiens | P27540 (AlphaFold model) |
>3F1P_1 Endothelial PAS domain-containing protein 1 (chains A) GEFKGLDSKTFLSEHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSH QNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKN
>3F1P_2 Aryl hydrocarbon receptor nuclear translocator (chains B) GEFKGLNVCQPTRFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLR DSFQQVVKLKGQVLSVMFRFRSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQ E
Artificial ligand binding within the HIF2alpha PAS-B domain of the HIF2 transcription factor. Scheuermann, T.H., Tomchick, D.R., Machius, M. et al. Proc Natl Acad Sci U S A (2009) 106:450-455. DOI 10.1073/pnas.0808092106 · PubMed
Other PDB entries of the same protein (UniProt Q99814 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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