9VRQ: FOXC2/NFAT1 complex

Crystal structure of FOXC2/NFAT1 complex bound to ARRE2 DNA. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 May 2026.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,939
Mol. weight: 57.72 kDa
Released: 20 May 2026

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

Secondary structure: helices and β-sheets

9VRQ contains 13 α-helices and 29 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: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	77-87	11
β-strand	92-93	2	1
α-helix	95-105	11
α-helix	107-110	4
α-helix	113-126	14
β-strand	130-132	3	1
β-strand	146-148	3	1

Chain N: 9 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	404-405	2	2
β-strand	408-414	7	2
α-helix	415-417	3
β-strand	419	1	3
β-strand	423-424	2	4
α-helix	432-435	4
β-strand	442-446	5	2
β-strand	454-462	9	3
β-strand	470	1	3
β-strand	474-478	5	4
β-strand	489-493	5	3
β-strand	496-503	8	3
β-strand	504	1	2
α-helix	505-507	3
β-strand	510-512	3	2
β-strand	516-520	5	4
α-helix	523-526	4
β-strand	541-551	11	3
β-strand	557-563	7	3
α-helix	564	1
α-helix	566	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	627-630	4	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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Forkhead box protein C2	A	protein	103	Homo sapiens	Q99958 (AlphaFold model)
ARRE2-S	C	DNA	21	Homo sapiens
ARRE2-as	D	DNA	21	Homo sapiens
Nuclear factor of activated T-cells, cytoplasmic 2	N	protein	287	Homo sapiens	Q13469 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9VRQ_1 Forkhead box protein C2 (chains A)
GPKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNEC
FVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKD

Sequence of entity 2 (C), FASTA

>9VRQ_2 ARRE2-S (chains C)
TTAGGAAAATTTGTTTCATAG

Sequence of entity 3 (D), FASTA

>9VRQ_3 ARRE2-AS (chains D)
AACTATGAAACAAATTTTCCT

Sequence of entity 4 (N), FASTA

>9VRQ_4 Nuclear factor of activated T-cells, cytoplasmic 2 (chains N)
ASSVPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMEN
KPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEVPLEPKNNMRA
TIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQAASNPIECSQ
RSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKD
KSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV

Primary citation

FOXC2 represses NFAT1-dependent transcription through a DNA-facilitated protein-protein interaction. Chen, X., Wu, S., Yue, S. et al. Nucleic Acids Res (2026) 54. DOI 10.1093/nar/gkag367 · PubMed

Other PDB entries of the same protein (UniProt Q99958 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6AKP 2.32 Å, Crystal Structural of FOXC2 DNA binding domain bound to PC promoter
6AKO 2.4 Å, Crystal Structure of FOXC2 DBD Bound to DBE2 DNA
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
6LBM 2.84 Å, Crystal Structure of FOXC2-DBD bound to a palindromic DNA sequence
6O3T 3.06 Å, Structural basis of FOXC2 and DNA interactions
1D5V Solution structure of the forkhead domain of the adipocyte-transcription factor freac-11…

Browse structure collections

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