1S9K: Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site

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.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 5
Atoms: 3,887
Mol. weight: 56.65 kDa
Released: 14 Jun 2005

Explore 1S9K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain C: 8 helices, 26 β-strands

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

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	142-190	49

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	269-315	47

Molecules and chains

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)

Sequence of entity 1 (A), FASTA

>1S9K_1 Human IL-2 ARRE1 Promoter Element, Plus Strand (chains A)
TTTGAAAATATGTGTAATAG

Sequence of entity 2 (B), FASTA

>1S9K_2 Human IL-2 ARRE1 Promoter Element, Minus Strand (chains B)
AACTATTACACATATTTTCA

Sequence of entity 3 (C), FASTA

>1S9K_3 Nuclear factor of activated T-cells, cytoplasmic 2 (chains C)
WPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQI
FIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGI
LKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQRSAHELP
MVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQPNML
FVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV

Sequence of entity 4 (D), FASTA

>1S9K_4 Proto-oncogene protein c-fos (chains D)
RRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEK

Sequence of entity 5 (E), FASTA

>1S9K_5 Transcription factor AP-1 (chains E)
RKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQL

Primary citation

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:

8R3F 1.55 Å, C-terminal Rel-homology Domain of NFAT1
8R07 1.74 Å, C-terminal Rel-homology Domain of NFAT1
1P7H 2.6 Å, Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element
9VRT 2.64 Å, Crystal structure of FOXC2/NFAT1 complex bound to ARRE2-P DNA
9VS2 2.65 Å, Crystal structure of FOXC2/NFAT1 complex bound to ARRE3-P DNA
1A02 2.7 Å, Structure of the DNA binding domains of nfat, fos and jun bound to DNA
2AS5 2.7 Å, Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA.
8OW4 2.75 Å, 2.75 angstrom crystal structure of human NFAT1 with bound DNA
3QRF 2.8 Å, Structure of a domain-swapped FOXP3 dimer
9VRQ 2.8 Å, Crystal structure of FOXC2/NFAT1 complex bound to ARRE2 DNA
1OWR 3.0 Å, Crystal structure of human NFAT1 bound monomerically to DNA
2O93 3.05 Å, Crystal structure of NFAT bound to the HIV-1 LTR tandem kappaB enhancer element

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