NMR solution structure of PHD finger fragment of Yeast Yng1 protein in free state. Determined by solution NMR. Released 3 Jul 2007.
Explore 2JMI in 3D Show helices and sheets RCSB PDB PDBe
2JMI contains 1 α-helix and 2 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 |
|---|---|---|---|
| β-strand | 39-40 | 2 | 1 |
| β-strand | 52-53 | 2 | 1 |
| α-helix | 71-79 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein YNG1 | A | protein | 90 | Saccharomyces cerevisiae | Q08465 (AlphaFold model) |
>2JMI_1 Protein YNG1 (chains A) GPLGSHMASEFINQGDVTEGNNNQEEVYCFCRNVSYGPMVACDNPACPFEWFHYGCVGLK QAPKGKWYCSKDCKEIANQRSKSKRQKRRK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Taverna, S.D., Ilin, S., Rogers, R.S. et al. Mol Cell (2006) 24:785-796. DOI 10.1016/j.molcel.2006.10.026 · PubMed
Other PDB entries of the same protein (UniProt Q08465 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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