Research workbench
Structure of the RSC4 tandem bromodomain in complex with an acetylated H3 peptide
Analyse Structure of the RSC4 tandem bromodomain in complex with an acetylated H3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R0Y
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromatin structure-remodeling complex protein RSC4
- UniProt
- Q02206
- Ligands
- ALY
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromatin structure-remodeling complex protein RSC4 | protein | 283 | 62% helix, 1% strand | Q02206 |
Ligands and binding sites
- ALY · N(6)-acetyllysine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 364 | 0.76 | 0.86 | 32 | empty |
| 2 | 243 | 0.59 | 0.79 | 28 | empty |
| 3 | 82 | 0.47 | 0.81 | 17 | empty |
| 4 | 67 | 0.46 | 0.83 | 16 | ALY |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 2R0Y · Structure of the Rsc4 tandem bromodomain in complex with an acetylated H3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q02206 · AlphaFold monomer V2.0 prediction for chromatin structure-remodeling complex subunit RSC4… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q02206
- Elsewhere: RCSB PDB 2R0Y · PDBe 2R0Y · UniProt Q02206
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