4O62: CW-type zinc finger of ZCWPW2

CW-type zinc finger of ZCWPW2 in complex with the amino terminus of histone H3. Determined by X-ray diffraction at 1.78 Å resolution. Released 26 Mar 2014.

Method
X-ray diffraction
Resolution
1.78 Å
Organism
Homo sapiens
Chains
4
Atoms
1,681
Mol. weight
22.73 kDa
Ligands
ZN
Released
26 Mar 2014

Explore 4O62 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4O62 contains 12 α-helices and 9 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.

Chains A and C: 4 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand2811
β-strand30-3232
β-strand41-4332
α-helix44-452
α-helix46-516
α-helix60-623
α-helix74-763
Chain B: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix26-283
β-strand29-3243
β-strand41-4333
α-helix46-516
α-helix60-623
α-helix74-774
Chain D: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3-533

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Zinc finger CW-type PWWP domain protein 2A, B, Cprotein59Homo sapiensQ504Y3 (AlphaFold model)
Histone H3.3Dprotein11Homo sapiensP84243 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>4O62_1 Zinc finger CW-type PWWP domain protein 2 (chains A, B, C)
GVENMYVNKVWVQCENENCLKWRLLSSEDSAKVDHDEPWYCFMNTDSRYNNCSISEEDF
Sequence of entity 2 (D), FASTA
>4O62_2 Histone H3.3 (chains D)
ARTKQTARKST

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn3

Water and common crystallization additives (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 Q504Y3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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