3E9G: Chromatin modification-related protein EAF3

Crystal structure long-form (residue1-124) of Eaf3 chromo domain. Determined by X-ray diffraction at 2.5 Å resolution. Released 4 Nov 2008.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
1,913
Mol. weight
30.18 kDa
Released
4 Nov 2008

Explore 3E9G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3E9G contains 6 α-helices and 14 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: 3 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand13-1861
β-strand21-32121
β-strand37-4041
β-strand5911
α-helix60-623
β-strand76-8161
α-helix86-883
β-strand90-9341
β-strand97-9821
α-helix102-12524
Chain B: 3 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand13-1862
β-strand21-32122
β-strand37-4042
β-strand5912
α-helix60-623
β-strand76-8162
α-helix86-883
β-strand90-9342
β-strand97-9932
α-helix102-12827

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chromatin modification-related protein EAF3A, Bprotein130Saccharomyces cerevisiaeQ12432 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3E9G_1 Chromatin modification-related protein EAF3 (chains A, B)
MVDLEQEFALGGRCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQK
LGEDESIPEEIINGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKK
SLLEHHHHHH

Primary citation

Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36. Sun, B., Hong, J., Zhang, P. et al. J Biol Chem (2008) 283:36504-36512. DOI 10.1074/jbc.M806564200 · PubMed

Other PDB entries of the same protein (UniProt Q12432 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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