Research workbench
DHP1 chromodomain Y24W variant bound to histone H3 peptide containing trimethyllysine
Analyse DHP1 chromodomain Y24W variant 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
- 6MHA
- Type
- protein
- Length
- 59 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heterochromatin protein 1; Histone H3 peptide containing trimethyllysine, H3K9ME3
- 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 |
| B | Histone H3 peptide containing trimethyllysine, H3K9ME3 | protein | 6 | 0% helix, 50% strand | — |
Interfaces
1 interface between chains.
- A–B · 562 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 6MHA · dHP1 Chromodomain Y24W variant bound to histone H3 peptide containing trimethyllysine · 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 6MHA · PDBe 6MHA · UniProt P05205
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