Research workbench
Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27.
Analyse Polycomb chromodomain complexed with the histone H3 tail containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PDQ
- Type
- protein
- Length
- 60 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polycomb protein; Histone H3.3
- UniProt
- P26017, P06351
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polycomb protein | protein | 51 | 24% helix, 51% strand | P26017 |
| B | Histone H3.3 | protein | 9 | 0% helix, 56% strand | P06351 |
Interfaces
1 interface between chains.
- A–B · 750 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 1PDQ · Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27. · the same entry in another collection · chain A against A, TM-score 1.00
- P26017 · AlphaFold monomer V2.0 prediction for polycomb group protein pc (P26017) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P26017
- Every structure of UniProt P06351
- Elsewhere: RCSB PDB 1PDQ · PDBe 1PDQ · UniProt P26017 · UniProt P06351
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