Structure analysis

Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site

X-ray diffraction
3.1Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero pentamer (preferred)
Entry contents: 3 distinct polypeptide molecules
2 distinct DNA molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero pentamer
Accessible surface area: 27111.98 Å2
Buried surface area: 9399.98 Å2
Dissociation area: 1,924.14 Å2
Dissociation energy (ΔGdiss): 18.14 kcal/mol
Dissociation entropy (TΔSdiss): 12.99 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-114582

Macromolecules

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Chain: D
Length: 53 amino acids
Theoretical weight: 6.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01100 (Residues: 140-192; Coverage: 14%)
Gene names: FOS, G0S7
Pfam: bZIP transcription factor
InterPro:
CATH: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
SCOP: Leucine zipper domain

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Name: Human IL-2 ARRE1 Promoter Element, Plus Strand
Representative chains: A
Length: 20 nucleotides
Theoretical weight: 6.21 KDa

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Name: Human IL-2 ARRE1 Promoter Element, Minus Strand
Representative chains: B
Length: 20 nucleotides
Theoretical weight: 6.05 KDa

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