MolNFT v1 · #105519 · protein
Crystal structure of RBBP4 bound to PHF6 peptide
4R7A · Phd finger protein 6: “Crystal structure of RBBP4 bound to PHF6 peptide”. X-ray diffraction, 4 pockets (best druggability 0.76). MolNFT v1 #105519 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4R7A
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phd finger protein 6; Histone-binding protein RBBP4
- UniProt
- Q8IWS0, Q09028
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 6 | protein | 9 | 0% helix, 0% strand | Q8IWS0 |
| B | Histone-binding protein RBBP4 | protein | 366 | 7% helix, 47% strand | Q09028 |
Ligands and binding sites
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.76 | 0.84 | 34 | empty |
| 2 | 56 | 0.43 | 0.82 | 16 | empty |
| 3 | 102 | 0.40 | 0.76 | 20 | empty |
| 4 | 103 | 0.36 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 634 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4R7A · Crystal Structure of RBBP4 bound to PHF6 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q09028 · AlphaFold monomer V2.0 prediction for histone-binding protein RBBP4 (Q09028) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q8IWS0 · AlphaFold monomer V2.0 prediction for phd finger protein 6 (Q8IWS0) · a predicted model of the same protein · chain A against A, TM-score 0.34
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 Q8IWS0
- Every structure of UniProt Q09028
- Elsewhere: RCSB PDB 4R7A · PDBe 4R7A · UniProt Q8IWS0 · UniProt Q09028
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