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Solution structures of the double phd fingers of human transcriptional protein DPF3 bound to a histone peptide containing acetylation at lysine 14

Analyse Solution structures of the double phd fingers of human transcriptional protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KWJ
Type: protein
Length: 134 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 · 16% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Histone peptide	protein	20	0% helix, 5% strand	—
A	Zinc finger protein DPF3	protein	114	18% helix, 11% 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 · 929 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

2KWJ · Solution structures of the double PHD fingers of human transcriptional protein DPF3 bound… · 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 0.88

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 2KWJ · PDBe 2KWJ · UniProt Q92784

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