Crystal structure long-form (residue1-124) of Eaf3 chromo domain. Determined by X-ray diffraction at 2.5 Å resolution. Released 4 Nov 2008.
Explore 3E9G in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-18 | 6 | 1 |
| β-strand | 21-32 | 12 | 1 |
| β-strand | 37-40 | 4 | 1 |
| β-strand | 59 | 1 | 1 |
| α-helix | 60-62 | 3 | |
| β-strand | 76-81 | 6 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-93 | 4 | 1 |
| β-strand | 97-98 | 2 | 1 |
| α-helix | 102-125 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-18 | 6 | 2 |
| β-strand | 21-32 | 12 | 2 |
| β-strand | 37-40 | 4 | 2 |
| β-strand | 59 | 1 | 2 |
| α-helix | 60-62 | 3 | |
| β-strand | 76-81 | 6 | 2 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-93 | 4 | 2 |
| β-strand | 97-99 | 3 | 2 |
| α-helix | 102-128 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chromatin modification-related protein EAF3 | A, B | protein | 130 | Saccharomyces cerevisiae | Q12432 (AlphaFold model) |
>3E9G_1 Chromatin modification-related protein EAF3 (chains A, B) MVDLEQEFALGGRCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQK LGEDESIPEEIINGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKK SLLEHHHHHH
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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