Solution Structure of ETO-TAFH refined in explicit solvent. Determined by solution NMR. Released 19 Jun 2007.
Explore 2PP4 in 3D Show helices and sheets RCSB PDB PDBe
2PP4 contains 5 α-helices and 0 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 | 120-140 | 21 | |
| α-helix | 144-156 | 13 | |
| α-helix | 162-173 | 12 | |
| α-helix | 181-203 | 23 | |
| α-helix | 207-217 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein ETO | A | protein | 107 | Homo sapiens | Q06455 (AlphaFold model) |
>2PP4_1 Protein ETO (chains A) GARQLSKLKRFLTTLQQYGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLR PFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTS
A TAF4-homology domain from the corepressor ETO is a docking platform for positive and negative regulators of transcription. Wei, Y., Liu, S., Lausen, J. et al. Nat Struct Mol Biol (2007) 14:653-661. DOI 10.1038/nsmb1258 · PubMed
Other PDB entries of the same protein (UniProt Q06455 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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