Research workbench
Decoding of methylated histone H3 tail by the pygo-BCL9 wnt signaling complex
Analyse Decoding of methylated histone H3 tail by the pygo-BCL9 wnt signaling complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VP7
- Type
- protein
- Length
- 98 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pygopus homolog 1; B-cell CLL/LYMPHOMA 9 protein
- UniProt
- Q9Y3Y4, O00512
- Ligands
- ZN, SO4
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pygopus homolog 1 | protein | 66 | 26% helix, 18% strand | Q9Y3Y4 |
| B | B-cell CLL/LYMPHOMA 9 protein | protein | 32 | 25% helix, 9% strand | O00512 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 672 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2VP7 · Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex · the same entry in another collection · chain A against A, 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 0.86
- 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 0.70
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 2VP7 · PDBe 2VP7 · UniProt Q9Y3Y4 · UniProt O00512
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