9VS2: FOXC2/NFAT1 complex

Crystal structure of FOXC2/NFAT1 complex bound to ARRE3-P DNA. Determined by X-ray diffraction at 2.65 Å resolution. Released 15 Jul 2026.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,964
Mol. weight: 57.72 kDa
Released: 15 Jul 2026

Explore 9VS2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VS2 contains 12 α-helices and 28 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.

Chain A: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	77-87	11
β-strand	93	1	6
α-helix	95-105	11
α-helix	107-109	3
α-helix	116-126	11
β-strand	130-132	3	6
β-strand	146-148	3	6
α-helix	150-154	5

Chain N: 7 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	404-405	2	1
β-strand	408-414	7	1
α-helix	415-417	3
β-strand	419	1	2
β-strand	423	1	3
α-helix	432-435	4
β-strand	442-446	5	1
β-strand	454-462	9	2
β-strand	470	1	2
β-strand	474-478	5	3
β-strand	489-493	5	2
β-strand	496-503	8	2
α-helix	505-507	3
β-strand	510-512	3	1
β-strand	516-520	5	3
α-helix	523-526	4
β-strand	541-551	11	2
β-strand	557-563	7	2
β-strand	567-568	2	2
α-helix	571-576	6
β-strand	579-583	5	4
β-strand	587-589	3	5
β-strand	595-601	7	4
β-strand	608-614	7	5
β-strand	620-626	7	5
β-strand	627-629	3	4
β-strand	637-641	5	4
α-helix	642-645	4
β-strand	654-661	8	5
β-strand	667	1	5
α-helix	669-670	2
β-strand	671-676	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ARRE3-P-S	C	DNA	21	Homo sapiens
ARRE3-P-as	D	DNA	21	Homo sapiens
Nuclear factor of activated T-cells, cytoplasmic 2	N	protein	287	Homo sapiens	Q13469 (AlphaFold model)
Forkhead box protein C2	A	protein	103	Homo sapiens	Q99958 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>9VS2_1 ARRE3-P-S (chains C)
TTAGGAAAATTTGTTTACTAG

Sequence of entity 2 (D), FASTA

>9VS2_2 ARRE3-P-AS (chains D)
CTAGTAAACAAATTTTCCTAA

Sequence of entity 3 (N), FASTA

>9VS2_3 Nuclear factor of activated T-cells, cytoplasmic 2 (chains N)
ASSVPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMEN
KPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEVPLEPKNNMRA
TIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQAASNPIECSQ
RSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKD
KSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV

Sequence of entity 4 (A), FASTA

>9VS2_4 Forkhead box protein C2 (chains A)
GPKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNEC
FVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKD

Primary citation

Crystal structure of FOXC2/NFAT1 complex bound to ARRE3-P DNA. Chen, X.J., Chen, Y.H. 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
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
1PZU 3.1 Å, An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site

Browse structure collections

About this viewer

MolViewer shows 9VS2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.