NMR solution structure of the C-myc-max heterodimeric leucine zipper, NMR, minimized average structure. Determined by solution NMR. Released 21 Oct 1998.
Explore 1A93 in 3D Show helices and sheets RCSB PDB PDBe
1A93 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 | 6-33 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myc proto-oncogene protein | A | protein | 34 | Homo sapiens | P01106 (AlphaFold model) |
| Max protein | B | protein | 34 | Mus musculus | P28574 (AlphaFold model) |
>1A93_1 MYC PROTO-ONCOGENE PROTEIN (chains A) XCGGVQAEEQKLISEEDLLRKRREQLKHKLEQLX
>1A93_2 MAX PROTEIN (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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