Research workbench
Solution structure of the bromodomain of human BRPF1 in complex with histone H4K5AC peptide
Analyse Solution structure of the bromodomain of human BRPF1 in complex with histone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RS9
- Type
- protein
- Length
- 131 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylated lysine 5 of peptide from histone H4; Peregrin
- UniProt
- P62805, P55201
Structure
solution nmr · 2 distinct chains · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetylated lysine 5 of peptide from histone H4 | protein | 10 | 0% helix, 0% strand | P62805 |
| B | Peregrin | protein | 121 | 63% helix, 0% strand | P55201 |
Interfaces
1 interface between chains.
- A–B · 397 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 2RS9 · Solution structure of the bromodomain of human BRPF1 in complex with histone H4K5ac… · the same entry in another collection · chain A against A, TM-score 1.00
- P55201 · AlphaFold monomer V2.0 prediction for peregrin (P55201) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 P62805
- Every structure of UniProt P55201
- Elsewhere: RCSB PDB 2RS9 · PDBe 2RS9 · UniProt P62805 · UniProt P55201
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