NMR study of C-jun homodimer. Determined by solution NMR. Released 20 Jun 1996.
Explore 1JUN in 3D Show helices and sheets RCSB PDB PDBe
1JUN contains 2 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 276-312 | 37 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C-jun homodimer | A, B | protein | 44 | Homo sapiens | P05412 (AlphaFold model) |
>1JUN_1 C-JUN HOMODIMER (chains A, B) XCGGRIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNY
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. Junius, F.K., O'Donoghue, S.I., Nilges, M. et al. J Biol Chem (1996) 271:13663-13667. DOI 10.1074/jbc.271.23.13663 · PubMed
Other PDB entries of the same protein (UniProt P05412 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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