1R05: Max B-HLH-LZ

Solution Structure of Max B-HLH-LZ. Determined by solution NMR. Released 21 Oct 2003.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,424
Mol. weight
20.35 kDa
Released
21 Oct 2003

Explore 1R05 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1R05 contains 10 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: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix18-2912
α-helix33-364
α-helix42-498
α-helix50-545
α-helix55-8228

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Max proteinA, Bprotein87Homo sapiensP61244 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1R05_1 Max protein (chains A, B)
MADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKVHT
LQQDIDDLKRQNALLEQQVRALEGSGC

Primary citation

The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors. Sauv, S., Tremblay, L., Lavigne, P. J Mol Biol (2004) 342:813-832. DOI 10.1016/j.jmb.2004.07.058 · PubMed

Other PDB entries of the same protein (UniProt P61244 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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