Decoding of methylated histone H3 tail by the pygo-BCL9 wnt signaling complex

Structure

x-ray diffraction · 4 distinct chains · 30% helix, 22% strand (DSSP).

Ligands and binding sites

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

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

Pockets

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

Interfaces

6 interfaces between chains.

• C–D · 692 Ų buried · 10 hydrogen bonds · protein-protein
• A–B · 676 Ų buried · 9 hydrogen bonds · protein-protein
• B–D · 539 Ų buried · 11 hydrogen bonds · protein-protein
• A–C · 532 Ų buried · 8 hydrogen bonds · protein-protein
• A–D · 117 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 2VPD · Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex · the same entry in another collection · chain D against D, TM-score 1.00
• Q9Y3Y4 · AlphaFold monomer V2.0 prediction for pygopus homolog 1 (Q9Y3Y4) · a predicted model of the same protein · chain A against A, TM-score 0.95
• O00512 · AlphaFold monomer V2.0 prediction for B-cell CLL/LYMPHOMA 9 protein (O00512) · a predicted model of the same protein · chain B against A, TM-score 0.74

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 Q9Y3Y4
• Every structure of UniProt O00512
• Elsewhere: RCSB PDB 2VPD · PDBe 2VPD · UniProt Q9Y3Y4 · UniProt O00512