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Solution structures of the double phd fingers of human transcriptional protein DPF3B bound to a H3 peptide wild type

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
2KWK
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
Pockets
1 · best druggability 0.43

Structure

solution nmr · 2 distinct chains · 16% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BHistone peptideprotein200% helix, 5% strand—
AZinc finger protein DPF3protein11418% helix, 10% strandQ92784

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.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.430.7922empty

Interfaces

1 interface between chains.

  • B–A · 609 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 2KWK · Solution structures of the double PHD fingers of human transcriptional protein DPF3b… · 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 0.89

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