Research workbench
RNA-RNA base stacking in the crystal structure of an HFQ6:RNA dimer
Analyse RNA-RNA base stacking in the crystal structure of an HFQ6:RNA dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NEW
- Type
- protein + RNA
- Length
- 136 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B7MKX6
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 64 | — | B7MKX6 |
| H | — | rna | 6 | — | — |
| C | — | rna | 2 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NEW · RNA-RNA base stacking in the crystal structure of an Hfq6:RNA dimer · the same entry in another collection · chain A against A, TM-score 1.00
- B7MKX6 · AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (B7MKX6) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 B7MKX6
- Elsewhere: RCSB PDB 5NEW · PDBe 5NEW · UniProt B7MKX6
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