NMR solution structure of the C-myc-max heterodimeric leucine zipper, 40 structures. Determined by solution NMR. Released 27 Jan 1999.
Explore 2A93 in 3D Show helices and sheets RCSB PDB PDBe
2A93 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 | 6-32 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-31 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C-myc-max heterodimeric leucine zipper | A | protein | 34 | P01106 (AlphaFold model) | |
| C-myc-max heterodimeric leucine zipper | B | protein | 34 | P28574 (AlphaFold model) |
>2A93_1 C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER (chains A) XCGGVQAEEQKLISEEDLLRKRREQLKHKLEQLX
>2A93_2 C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER (chains B) XCGGMRRKNDTHQQDIDDLKRQNALLEQQVRALX
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. Lavigne, P., Crump, M.P., Gagne, S.M. et al. J Mol Biol (1998) 281:165-181. DOI 10.1006/jmbi.1998.1914 · PubMed
Other PDB entries of the same protein (UniProt P01106 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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