Research workbench
Solution structure of the chromodomain of CHP1 in complex with H3K9ME3 peptide
Analyse Solution structure of the chromodomain of CHP1 in complex with H3K9ME3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RSN
- Type
- protein
- Length
- 93 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromo domain-containing protein 1; Peptide from histone H3
- UniProt
- Q10103
Structure
solution nmr · 2 distinct chains · 22% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromo domain-containing protein 1 | protein | 75 | 27% helix, 31% strand | Q10103 |
| B | Peptide from histone H3 | protein | 18 | 0% helix, 17% strand | — |
Interfaces
1 interface between chains.
- A–B · 724 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 2RSN · Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q10103 · AlphaFold monomer V2.0 prediction for chromo domain-containing protein 1 (Q10103) · a predicted model of the same protein · chain A against A, TM-score 0.66
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 Q10103
- Elsewhere: RCSB PDB 2RSN · PDBe 2RSN · UniProt Q10103
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