1A93: Myc proto-oncogene protein

NMR solution structure of the C-myc-max heterodimeric leucine zipper, NMR, minimized average structure. Determined by solution NMR. Released 21 Oct 1998.

Method
Solution NMR
Organisms
Homo sapiens, Mus musculus
Chains
2
Atoms
533
Mol. weight
7.62 kDa
Released
21 Oct 1998

Explore 1A93 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and B: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix6-3328

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myc proto-oncogene proteinAprotein34Homo sapiensP01106 (AlphaFold model)
Max proteinBprotein34Mus musculusP28574 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1A93_1 MYC PROTO-ONCOGENE PROTEIN (chains A)
XCGGVQAEEQKLISEEDLLRKRREQLKHKLEQLX
Sequence of entity 2 (B), FASTA
>1A93_2 MAX PROTEIN (chains B)
XCGGMRRKNDTHQQDIDDLKRQNALLEQQVRALX

Primary citation

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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