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.
Explore 2KWN in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 262 | 1 | 1 |
| β-strand | 268 | 1 | 2 |
| β-strand | 271 | 1 | 2 |
| β-strand | 290 | 1 | 1 |
| α-helix | 293-296 | 4 | |
| α-helix | 300-308 | 9 | |
| α-helix | 314-316 | 3 | |
| β-strand | 319 | 1 | 3 |
| β-strand | 331-333 | 3 | 3 |
| β-strand | 340-342 | 3 | 3 |
| α-helix | 360-370 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone peptide | B | protein | 15 | P62805 (AlphaFold model) | |
| Zinc finger protein DPF3 | A | protein | 114 | Homo sapiens | Q92784 (AlphaFold model) |
>2KWN_1 Histone peptide (chains B) GLGKGGAKRHRKVLR
>2KWN_2 Zinc finger protein DPF3 (chains A) GSYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKS CILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKAS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
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:
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