2RNZ: Histone acetyltransferase ESA1

Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1. Determined by solution NMR. Released 29 Apr 2008.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
777
Mol. weight
11.07 kDa
Released
29 Apr 2008

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

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix18-203
β-strand25-3061
β-strand35-44101
β-strand51-5551
β-strand65-6841
β-strand7211
α-helix77-793

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase ESA1Aprotein94Saccharomyces cerevisiaeQ08649 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2RNZ_1 Histone acetyltransferase ESA1 (chains A)
MGSSHHHHHHSSGLVPRGSHMSVDDIIIKCQCWVQKNDEERLAEILSINTRKAPPKFYVH
YVNYNKRLDEWITTDRINLDKEVLYPKLKATDED

Primary citation

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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