2JMI: Protein YNG1

NMR solution structure of PHD finger fragment of Yeast Yng1 protein in free state. Determined by solution NMR. Released 3 Jul 2007.

Method
Solution NMR
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
482
Mol. weight
10.4 kDa
Ligands
ZN
Released
3 Jul 2007

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

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 2 β-strands

ElementResiduesLengthSheet
β-strand39-4021
β-strand52-5321
α-helix71-799

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein YNG1Aprotein90Saccharomyces cerevisiaeQ08465 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JMI_1 Protein YNG1 (chains A)
GPLGSHMASEFINQGDVTEGNNNQEEVYCFCRNVSYGPMVACDNPACPFEWFHYGCVGLK
QAPKGKWYCSKDCKEIANQRSKSKRQKRRK

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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