MolNFT v1 · #49848 · protein
Structure of the RSC4 tandem bromodomain in complex with an acetylated H3 peptide
2R0Y · Chromatin structure-remodeling complex protein RSC4: “Structure of the RSC4 tandem bromodomain in complex with an acetylated H3 peptide”. X-ray diffraction, 1 ligand (ALY), 4 pockets (best druggability 0.76). MolNFT v1 #49848 on…
- 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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