Research workbench
Crystal structure of RBBP4: ZNF827 and its function in telomere
Analyse Crystal structure of RBBP4: ZNF827 and its function in telomere in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XXQ
- Type
- protein
- Length
- 780 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-binding protein RBBP4; Zinc finger protein 827
- UniProt
- Q09028
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-binding protein RBBP4 | protein | 380 | 9% helix, 46% strand | Q09028 |
| B | Histone-binding protein RBBP4 | protein | 380 | 9% helix, 44% strand | Q09028 |
| C, D | Zinc finger protein 827 | protein | 10 | 0% helix, 0% strand | — |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.75 | 0.81 | 55 | empty |
| 2 | 418 | 0.73 | 0.83 | 32 | empty |
| 3 | 387 | 0.68 | 0.81 | 68 | empty |
| 4 | 93 | 0.32 | 0.73 | 20 | empty |
| 5 | 63 | 0.30 | 0.75 | 19 | empty |
Interfaces
4 interfaces between chains.
- A–B · 922 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 728 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 701 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 120 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5XXQ · Crystal structure of RBBP4: ZNF827 and its function in telomere · 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
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 Q09028
- Elsewhere: RCSB PDB 5XXQ · PDBe 5XXQ · UniProt Q09028
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