Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site. Determined by X-ray diffraction at 3.1 Å resolution. Released 14 Jun 2005.
Explore 1S9K in 3D Show helices and sheets RCSB PDB PDBe
1S9K contains 10 α-helices and 26 β-strands across 3 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 | 404 | 1 | 1 |
| β-strand | 409-414 | 6 | 2 |
| α-helix | 415-417 | 3 | |
| β-strand | 419 | 1 | 3 |
| β-strand | 423 | 1 | 4 |
| α-helix | 428-432 | 5 | |
| β-strand | 442-446 | 5 | 2 |
| β-strand | 454-461 | 8 | 1 |
| β-strand | 470 | 1 | 1 |
| β-strand | 474-478 | 5 | 4 |
| β-strand | 491-492 | 2 | 1 |
| β-strand | 498-503 | 6 | 1 |
| α-helix | 505-507 | 3 | |
| β-strand | 510-512 | 3 | 2 |
| β-strand | 516-520 | 5 | 4 |
| α-helix | 523-526 | 4 | |
| β-strand | 541-542 | 2 | 3 |
| β-strand | 543-551 | 9 | 1 |
| β-strand | 557-563 | 7 | 1 |
| β-strand | 567-568 | 2 | 3 |
| α-helix | 571-576 | 6 | |
| β-strand | 579-583 | 5 | 5 |
| β-strand | 587-589 | 3 | 6 |
| β-strand | 595-601 | 7 | 5 |
| β-strand | 608-614 | 7 | 6 |
| β-strand | 620-626 | 7 | 6 |
| β-strand | 627-628 | 2 | 5 |
| β-strand | 637-641 | 5 | 5 |
| α-helix | 642-645 | 4 | |
| β-strand | 654-661 | 8 | 6 |
| β-strand | 667 | 1 | 6 |
| α-helix | 668-670 | 3 | |
| β-strand | 671-676 | 6 | 6 |
| α-helix | 677 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 142-190 | 49 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 269-315 | 47 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human IL-2 ARRE1 Promoter Element, Plus Strand | A | DNA | 20 | ||
| Human IL-2 ARRE1 Promoter Element, Minus Strand | B | DNA | 20 | ||
| Nuclear factor of activated T-cells, cytoplasmic 2 | C | protein | 280 | Homo sapiens | Q13469 (AlphaFold model) |
| Proto-oncogene protein c-fos | D | protein | 53 | Homo sapiens | P01100 (AlphaFold model) |
| Transcription factor AP-1 | E | protein | 52 | Homo sapiens | P05412 (AlphaFold model) |
>1S9K_1 Human IL-2 ARRE1 Promoter Element, Plus Strand (chains A) TTTGAAAATATGTGTAATAG
>1S9K_2 Human IL-2 ARRE1 Promoter Element, Minus Strand (chains B) AACTATTACACATATTTTCA
>1S9K_3 Nuclear factor of activated T-cells, cytoplasmic 2 (chains C) WPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQI FIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGI LKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQRSAHELP MVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQPNML FVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV
>1S9K_4 Proto-oncogene protein c-fos (chains D) RRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEK
>1S9K_5 Transcription factor AP-1 (chains E) RKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQL
Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site. Wang, D., Stroud, J.C., Chen, L. To be published.
Other PDB entries of the same protein (UniProt Q13469 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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