Research workbench
Crystal structure of aquifex aeolicus hfq-RNA complex at 1.5A
Analyse Crystal structure of aquifex aeolicus hfq-RNA complex at 1.5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SZE
- Type
- protein + RNA
- Length
- 73 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O66512
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 71 | — | O66512 |
| C | — | rna | 2 | — | — |
Ligands and binding sites
- MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- O66512 · AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (O66512) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O66512
- Elsewhere: RCSB PDB 5SZE · PDBe 5SZE · UniProt O66512
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