Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1. Determined by solution NMR. Released 29 Apr 2008.
Explore 2RNZ in 3D Show helices and sheets RCSB PDB PDBe
2RNZ contains 2 α-helices and 5 β-strands across 1 chain. 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 | 18-20 | 3 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 35-44 | 10 | 1 |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 65-68 | 4 | 1 |
| β-strand | 72 | 1 | 1 |
| α-helix | 77-79 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase ESA1 | A | protein | 94 | Saccharomyces cerevisiae | Q08649 (AlphaFold model) |
>2RNZ_1 Histone acetyltransferase ESA1 (chains A) MGSSHHHHHHSSGLVPRGSHMSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVH YVNYNKRLDEWITTDRINLDKEVLYPKLKATDED
Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain. Shimojo, H., Sano, N., Moriwaki, Y. et al. J Mol Biol (2008) 378:987-1001. DOI 10.1016/j.jmb.2008.03.021 · PubMed
Other PDB entries of the same protein (UniProt Q08649 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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