4QQ4: CW-type zinc finger of MORC3

CW-type zinc finger of MORC3 in complex with the amino terminus of histone H3. Determined by X-ray diffraction at 1.75 Å resolution. Released 20 Aug 2014.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
4
Atoms
1,045
Mol. weight
18.24 kDa
Ligands
ZN
Released
20 Aug 2014

Explore 4QQ4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QQ4 contains 8 α-helices and 6 β-strands across 4 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, 2 β-strands

ElementResiduesLengthSheet
α-helix4071
β-strand408-41251
β-strand419-42241
α-helix426-4305
α-helix435-4373
α-helix441-4433
α-helix449-4524
Chain B: 3 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix4071
β-strand408-41252
β-strand419-42242
α-helix435-4373
α-helix449-4524
Chains C and D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3-641

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MORC family CW-type zinc finger protein 3A, Bprotein62Homo sapiensQ14149 (AlphaFold model)
Histone H3.3C, Dprotein16Homo sapiensP84243 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4QQ4_1 MORC family CW-type zinc finger protein 3 (chains A, B)
GEDIQKRPDQTWVQCDACLKWRKLPDGMDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLV
HP
Sequence of entity 2 (C, D), FASTA
>4QQ4_2 Histone H3.3 (chains C, D)
ARTKQTARKSTGGKAX

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn3

Water and common crystallization additives (CL, UNX) are not listed.

Primary citation

Family-wide Characterization of Histone Binding Abilities of Human CW Domain-containing Proteins. Liu, Y., Tempel, W., Zhang, Q. et al. J Biol Chem (2016) 291:9000-9013. DOI 10.1074/jbc.M116.718973 · PubMed

Other PDB entries of the same protein (UniProt Q14149 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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