Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex. Determined by X-ray diffraction at 2.77 Å resolution. Released 17 Jun 2008.
Explore 2VPD in 3D Show helices and sheets RCSB PDB PDBe
2VPD contains 9 α-helices and 14 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 342 | 1 | 1 |
| β-strand | 349 | 1 | 1 |
| β-strand | 356-358 | 3 | 2 |
| β-strand | 366-368 | 3 | 2 |
| α-helix | 369-372 | 4 | |
| α-helix | 376-384 | 9 | |
| β-strand | 388-390 | 3 | 3 |
| α-helix | 393-397 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 173-180 | 8 | 3 |
| α-helix | 182-193 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 338-340 | 3 | |
| β-strand | 341-342 | 2 | 4 |
| β-strand | 343 | 1 | 5 |
| β-strand | 349-350 | 2 | 4 |
| β-strand | 356-358 | 3 | 5 |
| β-strand | 359 | 1 | 3 |
| β-strand | 366-368 | 3 | 5 |
| α-helix | 369-372 | 4 | |
| α-helix | 376-384 | 9 | |
| β-strand | 388-390 | 3 | 3 |
| α-helix | 393-396 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 172-180 | 9 | 3 |
| α-helix | 182-193 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Pygopus homolog 1 | A, C | protein | 67 | HOMO SAPIENS | Q9Y3Y4 (AlphaFold model) |
| B-cell cll/lymphoma 9 protein | B, D | protein | 35 | HOMO SAPIENS | O00512 (AlphaFold model) |
>2VPD_1 PYGOPUS HOMOLOG 1 (chains A, C) MGHSSSDPVYPCGICTNEVNDDQDAILCEASCQKWFHRICTGMTETAYGLLTAEASAVWG CDTCMAD
>2VPD_2 B-CELL CLL/LYMPHOMA 9 PROTEIN (chains B, D) AMAAKVVYVFSTEMANKAAEAVLKGQVETIVSFHI
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Decoding of Methylated Histone H3 Tail by the Pygo- Bcl9 Wnt Signaling Complex. Fiedler, M., Sanchez-Barrena, M.J., Nekrasov, M. et al. Mol Cell (2008) 30:507. DOI 10.1016/J.MOLCEL.2008.03.011 · PubMed
Other PDB entries of the same protein (UniProt Q9Y3Y4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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