4LJN: MOZ double PHD finger

Crystal Structure of MOZ double PHD finger. Determined by X-ray diffraction at 3.0 Å resolution. Released 16 Oct 2013.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Homo sapiens
Chains
1
Atoms
945
Mol. weight
15.76 kDa
Ligands
ZN
Released
16 Oct 2013

Explore 4LJN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LJN contains 6 α-helices and 6 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: 6 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix195-1984
α-helix203-2064
β-strand20911
α-helix226-2272
β-strand228-22921
β-strand236-23721
α-helix246-2538
β-strand26512
β-strand278-28032
β-strand287-28932
α-helix290-2923
α-helix296-2972

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase KAT6AAprotein136Homo sapiensQ92794 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4LJN_1 Histone acetyltransferase KAT6A (chains A)
GSHMLELPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPE
LTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWIC
QICRPRKKGRKLLQKK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

The double PHD finger domain of MOZ/MYST3 induces alpha-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Dreveny, I., Deeves, S.E., Fulton, J. et al. Nucleic Acids Res (2014) 42:822-835. DOI 10.1093/nar/gkt931 · PubMed

Other PDB entries of the same protein (UniProt Q92794 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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