Research workbench
Structure of HSTAU1 DSRBD3-4 in complex with ARF1 RNA
Analyse Structure of HSTAU1 DSRBD3-4 in complex with ARF1 RNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HTU
- Type
- protein + RNA
- Length
- 255 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA (19-mer); Double-stranded RNA-binding protein staufen homolog 1
- UniProt
- O95793
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | RNA (19-mer) | rna | 19 | — | — |
| F | RNA (19-mer) | rna | 19 | — | — |
| A, B | Double-stranded RNA-binding protein staufen homolog 1 | protein | 76 | 39% helix, 32% strand | O95793 |
| C | Double-stranded RNA-binding protein staufen homolog 1 | protein | 65 | 25% helix, 23% strand | O95793 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 979 | 0.76 | 0.79 | 63 | empty |
| 2 | 58 | 0.61 | 0.93 | 16 | empty |
| 3 | 121 | 0.38 | 0.74 | 18 | empty |
| 4 | 61 | 0.36 | 0.78 | 17 | empty |
| 5 | 59 | 0.35 | 0.79 | 13 | empty |
Interfaces
8 interfaces between chains.
- D–F · 905 Ų buried · 80 hydrogen bonds · nucleic-nucleic
- D–A · 474 Ų buried · 7 hydrogen bonds · protein-nucleic
- F–A · 398 Ų buried · 5 hydrogen bonds · protein-nucleic
- F–B · 391 Ų buried · 5 hydrogen bonds · protein-nucleic
- A–C · 269 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6HTU · Structure of hStau1 dsRBD3-4 in complex with ARF1 RNA · the same entry in another collection · chain F against F, TM-score 1.00
- O95793 · AlphaFold monomer V2.0 prediction for double-stranded RNA-binding protein staufen homolog… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O95793
- Elsewhere: RCSB PDB 6HTU · PDBe 6HTU · UniProt O95793
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