Research workbench
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
Analyse Solution structure of the double phd (plant homeodomain) fingers of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KWN
- Type
- protein
- Length
- 129 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone peptide; Zinc finger protein DPF3
- UniProt
- Q92784
- Ligands
- ZN
Structure
solution nmr · 2 distinct chains · 21% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Histone peptide | protein | 15 | 0% helix, 0% strand | — |
| A | Zinc finger protein DPF3 | protein | 114 | 24% helix, 10% strand | Q92784 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 715 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 2KWN · Solution structure of the double PHD (plant homeodomain) fingers of human transcriptional… · the same entry in another collection · chain B against B, TM-score 1.00
- Q92784 · AlphaFold monomer V2.0 prediction for zinc finger protein DPF3 (Q92784) · a predicted model of the same protein · chain A against A, TM-score 0.83
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q92784
- Elsewhere: RCSB PDB 2KWN · PDBe 2KWN · UniProt Q92784
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