5B79: DPF2 double PHD finger

Crystal structure of DPF2 double PHD finger. Determined by X-ray diffraction at 2.6 Å resolution. Released 26 Oct 2016.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
1
Atoms
928
Mol. weight
14.08 kDa
Ligands
ZN
Released
26 Oct 2016

Explore 5B79 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5B79 contains 8 α-helices and 5 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: 8 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand34-3521
β-strand42-4321
α-helix52-576
α-helix66-683
β-strand7112
α-helix80-823
β-strand83-8532
α-helix861
β-strand92-9432
α-helix101-1022
α-helix105-1062
α-helix113-1197
α-helix120-1223

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Zinc finger protein ubi-d4Aprotein123Homo sapiensQ92785 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5B79_1 Zinc finger protein ubi-d4 (chains A)
SNNYCDFCLGDSKINKKTGQPEELVSCSDCGRSGHPSCLQFTPVMMAAVKTYRWQCIECK
CCNICGTSENDDQLLFCDDCDRGYHMYCLTPSMSEPPEGSWSCHLCLDLLKEKASIYQNQ
NSS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2. Xiong, X., Panchenko, T., Yang, S. et al. Nat Chem Biol (2016) 12:1111-1118. DOI 10.1038/nchembio.2218 · PubMed

Other PDB entries of the same protein (UniProt Q92785 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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