Research workbench
Chromodomain HP1 with Y24F mutation bound to histone H3 peptide containing trimethyl lysine
Analyse Chromodomain HP1 with Y24F mutation bound to histone H3 peptide containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ASZ
- Type
- protein
- Length
- 59 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heterochromatin protein 1; Trimethyl lysine histone H3 tail peptide
- UniProt
- P05205
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heterochromatin protein 1 | protein | 53 | 30% helix, 51% strand | P05205 |
| P | Trimethyl lysine histone H3 tail peptide | protein | 6 | 0% helix, 50% strand | — |
Interfaces
1 interface between chains.
- A–P · 597 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 6ASZ · Chromodomain HP1 with Y24F mutation bound to histone H3 peptide containing trimethyl… · the same entry in another collection · chain A against A, TM-score 1.00
- P05205 · AlphaFold monomer V2.0 prediction for heterochromatin protein 1 (P05205) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P05205
- Elsewhere: RCSB PDB 6ASZ · PDBe 6ASZ · UniProt P05205
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