2A93: C-myc-max heterodimeric leucine zipper

NMR solution structure of the C-myc-max heterodimeric leucine zipper, 40 structures. Determined by solution NMR. Released 27 Jan 1999.

Method
Solution NMR
Chains
2
Atoms
533
Mol. weight
7.62 kDa
Released
27 Jan 1999

Explore 2A93 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix6-3227
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix6-3126

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
C-myc-max heterodimeric leucine zipperAprotein34P01106 (AlphaFold model)
C-myc-max heterodimeric leucine zipperBprotein34P28574 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2A93_1 C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER (chains A)
XCGGVQAEEQKLISEEDLLRKRREQLKHKLEQLX
Sequence of entity 2 (B), FASTA
>2A93_2 C-MYC-MAX HETERODIMERIC LEUCINE ZIPPER (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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