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Crystal structure analysis of the phd domain of the transcription coactivator pygophus

Analyse Crystal structure analysis of the phd domain of the transcription coactivator… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2DX8
Type
protein
Length
120 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pygopus homolog 1
UniProt
Q9D0P5
Ligands
ZN
Pockets
2 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPygopus homolog 1protein6023% helix, 18% strandQ9D0P5

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.320.7718empty
2550.310.7612empty

Interfaces

1 interface between chains.

  • A–B · 483 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 2DX8 · Crystal Structure Analysis of the PHD domain of the Transcription Coactivator Pygophus · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9D0P5 · AlphaFold monomer V2.0 prediction for pygopus homolog 1 (Q9D0P5) · a predicted model of the same protein · chain A against A, TM-score 0.96

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