2JMJ: PHD domain from the yeast YNG1 protein

NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide. Determined by solution NMR. Released 3 Jul 2007.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
558
Mol. weight
11.51 kDa
Ligands
ZN
Released
3 Jul 2007

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

Secondary structure: helices and β-sheets

2JMJ contains 1 α-helix and 5 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: 1 helix, 4 β-strands

ElementResiduesLengthSheet
β-strand2711
β-strand3411
β-strand39-4022
β-strand52-5322
α-helix71-788
Chain P: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3-422

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein YNG1Aprotein90Saccharomyces cerevisiaeQ08465 (AlphaFold model)
Histone H3Pprotein9P61830 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JMJ_1 Protein YNG1 (chains A)
GPLGSHMASEFINQGDVTEGNNNQEEVYCFCRNVSYGPMVACDNPACPFEWFHYGCVGLK
QAPKGKWYCSKDCKEIANQRSKSKRQKRRK
Sequence of entity 2 (P), FASTA
>2JMJ_2 Histone H3 (chains P)
ARTKQTARK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

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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