3V43: MOZ

Crystal structure of MOZ. Determined by X-ray diffraction at 1.47 Å resolution. Released 27 Jun 2012.

Method
X-ray diffraction
Resolution
1.47 Å
Organism
Homo sapiens
Chains
2
Atoms
1,092
Mol. weight
15.09 kDa
Ligands
ZN
Released
27 Jun 2012

Explore 3V43 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3V43 contains 5 α-helices and 7 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: 5 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix203-2064
β-strand20911
α-helix226-2272
β-strand228-22921
β-strand236-23721
α-helix239-2424
α-helix246-2538
β-strand26512
β-strand279-28022
β-strand287-28822
α-helix290-2923
Chain Q: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand2-322

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase KAT6AAprotein112Homo sapiensQ92794 (AlphaFold model)
Histone H3.1Qprotein18Homo sapiensP68431 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3V43_1 Histone acetyltransferase KAT6A (chains A)
HMEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIE
CKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPR
Sequence of entity 2 (Q), FASTA
>3V43_2 Histone H3.1 (chains Q)
ARTKQTARKSTGGKAPRK

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Water and common crystallization additives (ACT) are not listed.

Primary citation

Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription. Qiu, Y., Liu, L., Zhao, C. et al. Genes Dev (2012) 26:1376-1391. DOI 10.1101/gad.188359.112 · 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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