Research workbench
Structural basis of the interaction of RBAP46/RBAP48 with histone H4
Analyse Structural basis of the interaction of RBAP46/RBAP48 with histone H4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CFS
- Type
- protein
- Length
- 398 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-binding protein RBBP7; Histone H4
- UniProt
- Q16576, P62805
- Ligands
- ARS
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Histone-binding protein RBBP7 | protein | 383 | 9% helix, 44% strand | Q16576 |
| E | Histone H4 | protein | 15 | 67% helix, 0% strand | P62805 |
Ligands and binding sites
- ARS · Arsenic · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 475 | 0.77 | 0.85 | 32 | empty |
| 2 | 95 | 0.47 | 0.81 | 18 | empty |
| 3 | 104 | 0.44 | 0.78 | 16 | ARS |
| 4 | 75 | 0.43 | 0.81 | 14 | empty |
| 5 | 91 | 0.37 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- B–E · 729 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3CFS · Structural basis of the interaction of RbAp46/RbAp48 with histone H4 · the same entry in another collection · chain B against B, TM-score 1.00
- Q16576 · AlphaFold monomer V2.0 prediction for histone-binding protein RBBP7 (Q16576) · a predicted model of the same protein · chain B 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 Q16576
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 3CFS · PDBe 3CFS · UniProt Q16576 · UniProt P62805
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