Research workbench
Solution NMR structures of AF9 yeats domain in complex with histon H3 acetylation at K18
Analyse Solution NMR structures of AF9 yeats domain in complex with histon H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NDF
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein af-9; Histone H3 peptide
- UniProt
- P42568
Structure
solution nmr · 2 distinct chains · 8% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein af-9 | protein | 141 | 9% helix, 48% strand | P42568 |
| B | Histone H3 peptide | protein | 13 | 0% helix, 8% strand | — |
Interfaces
1 interface between chains.
- A–B · 538 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 2NDF · Solution NMR structures of AF9 yeats domain in complex with histon H3 acetylation at K18 · the same entry in another collection · chain A against A, TM-score 1.00
- P42568 · AlphaFold monomer V2.0 prediction for protein af-9 (P42568) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P42568
- Elsewhere: RCSB PDB 2NDF · PDBe 2NDF · UniProt P42568
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