Research workbench
Crystal structure of enl yeats domain T1 mutant in complex with histone H3 acetylation at K27
Analyse Crystal structure of enl yeats domain T1 mutant in complex with histone H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E7C
- Type
- protein
- Length
- 152 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein enl; Histone H3K27AC(24-27) peptide
- UniProt
- Q03111
- Ligands
- IOD
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein enl | protein | 148 | 8% helix, 49% strand | Q03111 |
| B | Histone H3K27AC(24-27) peptide | protein | 4 | 0% helix, 25% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 375 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 7E7C · Crystal structure of ENL YEATS domain T1 mutant in complex with histone H3 acetylation at… · the same entry in another collection · chain A against A, TM-score 1.00
- Q03111 · AlphaFold monomer V2.0 prediction for protein enl (Q03111) · 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 Q03111
- Elsewhere: RCSB PDB 7E7C · PDBe 7E7C · UniProt Q03111
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