Solution Structure of Max B-HLH-LZ. Determined by solution NMR. Released 21 Oct 2003.
Explore 1R05 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 18-29 | 12 | |
| α-helix | 33-36 | 4 | |
| α-helix | 42-49 | 8 | |
| α-helix | 50-54 | 5 | |
| α-helix | 55-82 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Max protein | A, B | protein | 87 | Homo sapiens | P61244 (AlphaFold model) |
>1R05_1 Max protein (chains A, B) MADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKVHT LQQDIDDLKRQNALLEQQVRALEGSGC
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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