1JUN: NMR study of C-jun homodimer

NMR study of C-jun homodimer. Determined by solution NMR. Released 20 Jun 1996.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
680
Mol. weight
9.77 kDa
Released
20 Jun 1996

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

Secondary structure: helices and β-sheets

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.

Chains A and B: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix276-31237

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
C-jun homodimerA, Bprotein44Homo sapiensP05412 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1JUN_1 C-JUN HOMODIMER (chains A, B)
XCGGRIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNY

Primary citation

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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