Research workbench
Chromodomain HP1 with a P-nitro-L-phenylalanine mutation at position 24 bound to histone H3 peptide containing trimethyl lysine
Analyse Chromodomain HP1 with a P-nitro-L-phenylalanine mutation at position 24 bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AT0
- 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 · 628 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation, nonstandard).
Compared structures
- 6AT0 · Chromodomain HP1 with a p-nitro-L-phenylalanine mutation at position 24 bound to histone… · 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 6AT0 · PDBe 6AT0 · UniProt P05205
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