2KWN: Histone peptide

Solution structure of the double PHD (plant homeodomain) fingers of human transcriptional protein DPF3b bound to a histone H4 peptide containing acetylation at Lysine 16. Determined by solution NMR. Released 14 Jul 2010.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,002
Mol. weight
14.69 kDa
Ligands
ZN
Released
14 Jul 2010

Explore 2KWN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KWN contains 4 α-helices and 7 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: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand26211
β-strand26812
β-strand27112
β-strand29011
α-helix293-2964
α-helix300-3089
α-helix314-3163
β-strand31913
β-strand331-33333
β-strand340-34233
α-helix360-37011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone peptideBprotein15P62805 (AlphaFold model)
Zinc finger protein DPF3Aprotein114Homo sapiensQ92784 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>2KWN_1 Histone peptide (chains B)
GLGKGGAKRHRKVLR
Sequence of entity 2 (A), FASTA
>2KWN_2 Zinc finger protein DPF3 (chains A)
GSYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKS
CILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKAS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b. Zeng, L., Zhang, Q., Li, S. et al. Nature (2010) 466:258-262. DOI 10.1038/nature09139 · PubMed

Other PDB entries of the same protein (UniProt P62805 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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